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D-lysine
L-lysine
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
D-serine
L-serine
-
-
-
-
r
L-2-Aminobutyrate
D-2-Aminobutyrate
0.37% of the activity with L-Ala
-
r
L-2-aminobutyric acid
D-2-aminobutyric acid
-
18% of the activity with L-Ala
-
?
L-alanine
R-alanine
-
-
-
r
L-Arg
D-Arg
-
stepwise mechanism for alanine racemase at both 25°C and at 65°C. The carbanionic intermediate is obligatory, and Arg219 may serve to destabilize it to avoid side reactions such as transamination, a detailed reaction mechanism is proposed that includes enzyme and substrate protonation states
-
r
L-arginine
D-arginine
less than 10% activity compared to L-alanine
-
-
r
L-isoleucine
D-isoleucine
L-Methionine
D-Methionine
less than 10% activity compared to L-alanine
-
-
r
L-phenylalanine
D-phenylalanine
1.1% activity compared to L-alanine
-
-
r
L-proline
D-proline
1.1% activity compared to L-alanine
-
-
r
L-valine
D-valine
less than 10% activity compared to L-alanine
-
-
r
additional information
?
-
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
Alkalihalophilus pseudofirmus
reversible racemization
-
-
r
D-alanine
L-alanine
Alkalihalophilus pseudofirmus OF4
reversible racemization
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
?
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
D-alanine
L-alanine
-
-
-
-
r
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-Ala
D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
specific for Ala
-
?
L-Ala
D-Ala
-
specific for Ala
-
?
L-Ala
D-Ala
-
the enzyme catalyzes transamination as a side function.The pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
-
r
L-Ala
D-Ala
-
Tyr265 and Lys39 are the catalytic bases removing alpha-hydrogen from L- and D-alanine
-
r
L-Ala
D-Ala
the enzyme catalyzes the first committed step in bacterial cell wall biosynthesis
-
?
L-Ala
D-Ala
-
highly specific for Ala
-
r
L-Ala
D-Ala
-
the ratio of the activity for conversion of D-alanine to L-alanine to that of the reverse conversion is constantly about 0.5 in the pH range 7-9.5
-
r
L-Ala
D-Ala
-
enzyme is required for production of D-Ala, a necessary component of the bacterial cell wall
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
-
-
r
L-alanine
D-alanine
Alkalihalophilus pseudofirmus
-
-
-
r
L-alanine
D-alanine
Alkalihalophilus pseudofirmus
reversible racemization
-
-
r
L-alanine
D-alanine
Alkalihalophilus pseudofirmus OF4
-
-
-
r
L-alanine
D-alanine
Alkalihalophilus pseudofirmus OF4
reversible racemization
-
-
r
L-alanine
D-alanine
Alkalihalophilus pseudofirmus OF4
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
Q81VF6
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
Q81VF6
-
enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
alanine racemase can discriminate effectively between L-alanine and L-2-aminobutyric acid, and selectively and reversibly catalyzes L-alanine to D-alanine transformation Therefore, the enzyme shows ability of eliminating L-Ala from the reaction mixtures of L-2-aminobutyric acid biosynthesis, method optimization and evaluation in a coupled reaction with D-amino acid oxidase converting D-alanine to pyruvate stereoselectively, overview
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
?
L-alanine
D-alanine
-
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
?
L-alanine
D-alanine
TOXG encodes an alanine racemase whose function is to synthesize D-Ala for incorporation into HC-toxin, enzyme is involved in cyclic peptide biosynthesis
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine, highly preferred substrate
-
-
r
L-alanine
D-alanine
reversible racemization
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
reversible racemization
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
reversible racemization
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
first step in the biosynthesis of the peptidoglycan
-
-
?
L-alanine
D-alanine
-
The bacterium utilizes D-alanine (DAla) for synthesis of the peptidoglycan cell wall.
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
a major component of the alanine pathway, D-alanine is a major component in cell wall synthesis
-
-
?
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
catalyzes the interconversion of D-alanine and L-alanine
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
optimal substrate for alanine racemase
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
optimal substrate for alanine racemase
-
-
?
L-alanine
D-alanine
-
-
-
-
?
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
?
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
-
r
L-alanine
D-alanine
-
responsible for the synthesis of the d-alanine moiety present in cyclosporin A and of HC-toxin
-
-
?
L-alanine
D-alanine
-
reversible reaction from an external aldimine in both directions via a quinonoid intermediate, overview
-
-
r
L-alanine
D-alanine
-
-
-
r
L-alanine
D-alanine
-
-
-
r
L-isoleucine
D-isoleucine
-
-
-
-
?
L-isoleucine
D-isoleucine
-
-
-
-
?
L-leucine
D-leucine
-
activity is 20% compared with L-alanine, other amino acids are not racemized
-
-
r
L-leucine
D-leucine
0.9% activity compared to L-alanine
-
-
r
L-lysine
D-lysine
less than 10% activity compared to L-alanine
-
-
r
L-lysine
D-lysine
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
L-Ser
D-Ser
-
50% of the activity with L-Ala
-
?
L-Ser
D-Ser
-
at 0.5% of the activity with L-Ala
-
?
L-Ser
D-Ser
-
40% of the activity with L-Ala
-
-
?
L-Ser
D-Ser
3.7% of the activity with L-Ala
-
r
L-Ser
D-Ser
2% of the activity with L-Ala
-
r
L-serine
D-serine
less than 10% activity compared to L-alanine
-
-
r
L-serine
D-serine
-
-
-
-
r
additional information
?
-
assay method optimization and validation, overview
-
-
?
additional information
?
-
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
assay method optimization and validation, overview
-
-
?
additional information
?
-
-
exchange of the alpha-hydrogen of D-Ala and L-Ala with D2O
-
-
?
additional information
?
-
high specificity to L-alanine, low activity with L-arginine, L-methionine, L-lysine, L-serine, L-valine, L-proline, L-phenylalanine, L-leucine, respectively, no activity with L-histidine
-
-
?
additional information
?
-
the enzyme is absolutely specific for L-alanine compared to other L-amino acids, overview
-
-
?
additional information
?
-
the Pelagibacter ubique cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity
-
-
-
additional information
?
-
-
the Pelagibacter ubique cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity
-
-
-
additional information
?
-
the Pelagibacter ubique cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine. The ALR activity of MBP-PuCBL is 40fold lower than its CBL activity
-
-
-
additional information
?
-
-
purified chlamydial GlyA also exhibits racemase activity on L-Ala in vitro
-
-
?
additional information
?
-
Alr2 can interconvert L- and D-serine and Alr2 binds to L- and D-serine with 2fold weaker affinity to that of L- and D-alanine, cf. EC 5.1.1.18
-
-
?
additional information
?
-
-
Alr2 can interconvert L- and D-serine and Alr2 binds to L- and D-serine with 2fold weaker affinity to that of L- and D-alanine, cf. EC 5.1.1.18
-
-
?
additional information
?
-
Alr2 converts L-serine to an approximately equal amount of D-serine. When tested with D-serine, Alr2 does not convert as much, and nearly 75% of the D-serine remains in the D-form
-
-
?
additional information
?
-
-
Alr2 converts L-serine to an approximately equal amount of D-serine. When tested with D-serine, Alr2 does not convert as much, and nearly 75% of the D-serine remains in the D-form
-
-
?
additional information
?
-
Alr2 can interconvert L- and D-serine and Alr2 binds to L- and D-serine with 2fold weaker affinity to that of L- and D-alanine, cf. EC 5.1.1.18
-
-
?
additional information
?
-
Alr2 converts L-serine to an approximately equal amount of D-serine. When tested with D-serine, Alr2 does not convert as much, and nearly 75% of the D-serine remains in the D-form
-
-
?
additional information
?
-
the Escherichia coli cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine
-
-
-
additional information
?
-
-
the Escherichia coli cystathionine beta-lyase (CBL, EC 4.4.1.13) also shows a promiscuous alanine racemase (ALR) activity. CBL catalyzes the beta-elimination of cystathionine
-
-
-
additional information
?
-
-
the enzyme catalyzes transamination as side reaction, R-isomer preference in the hydrogen abstraction from pyridoxamine 5'-phosphate
-
?
additional information
?
-
-
the epsilon-amino group of Lys39 participates in both racemization and transamination when catalyzed by the wild-type enzyme
-
?
additional information
?
-
residues Ile222 and Tyr354 are important for the enzyme substrate specificity
-
-
?
additional information
?
-
-
residues Ile222 and Tyr354 are important for the enzyme substrate specificity
-
-
?
additional information
?
-
-
no racemization of L-Ser, L-Asp, L-Glu, L-Val and L-Arg
-
?
additional information
?
-
-
the enzyme is only specific to L-alanine and L-isoleucine, and does not catalyze isomerization the other amino acids
-
-
?
additional information
?
-
-
the enzyme is only specific to L-alanine and L-isoleucine, and does not catalyze isomerization the other amino acids
-
-
?
additional information
?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
?
additional information
?
-
-
alr racemase is constitutive and serves an anabolic function, dadB encoded enzyme is inducible and required for cell growth on L-Ala
-
-
?
additional information
?
-
-
two nonhomologous alanine racemase genes, one of which is associated with the catabolic function and the other of which presumably represents the biosynthetic function
-
-
?
additional information
?
-
-
specific for alanine
-
-
?
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1)
-
-
-
additional information
?
-
-
TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1)
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1)
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1)
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
TmCBL is a substantially better GLR (EC 5.1.1.3) than an ALR (EC 5.1.1.1)
-
-
-
additional information
?
-
-
key enzyme in cyclosporin A biosynthesis
-
-
?
additional information
?
-
-
Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions, kinetic analysis and reaction mechanisms, overview
-
-
?
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
-
-
-
additional information
?
-
the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria
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FAD
-
not required as cofactor, slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q81VF6
-
pyridoxal 5'-phosphate
-
the monomeric inactive enzyme appears to bind the cofactor pyridoxal 5'-phosphate by a non-covalent linkage, although the native dimeric enzyme binds the cofactor through an aldimine Schiff base linkage
pyridoxal 5'-phosphate
-
1 pyridoxal 5'-phosphate per 42000 MW subunit
pyridoxal 5'-phosphate
-
not required as cofactor, slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated
pyridoxal 5'-phosphate
-
the sequence of 10 amino acid residues around the Lys residue, to which pyridoxal 5'-phosphate is bound, is identical with that of the dadB racemase
pyridoxal 5'-phosphate
-
1 mol of pyridoxal 5'-phosphate is bound per subunit
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
2 mol of pyridoxal 5'-phosphate bound per mol of enzyme dimer
pyridoxal 5'-phosphate
-
2 mol of pyridoxal 5'-phosphate bound per mol of enzyme dimer
pyridoxal 5'-phosphate
-
required as coenzyme
pyridoxal 5'-phosphate
-
required as coenzyme
pyridoxal 5'-phosphate
-
Arg219 forms a hydrogen bond with the pyridine nitrogen of the cofactor, Arg136 donates a hydrogen bond to the phenolic oxygen of pyridoxal 5'-phosphate and may be involved in the binding of substrate as well as stabilization of intermediates
pyridoxal 5'-phosphate
-
Km: 0.000033 mM
pyridoxal 5'-phosphate
-
contains one mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
cofactor
pyridoxal 5'-phosphate
coenzyme
pyridoxal 5'-phosphate
-
enzyme is dependent on
pyridoxal 5'-phosphate
-
1 mol per mol of enzyme
pyridoxal 5'-phosphate
-
1 mol of enzyme contains 2 mol of cofactor
pyridoxal 5'-phosphate
both active sites of the dimer contain a pyridoxal 5'-phosphate molecule in aldimine linkage to Lys39 as a protonated Schiff base. The protonated pyridoxal 5'-phosphate-Lys39 Schiff base is the reactive form of the enzyme
pyridoxal 5'-phosphate
each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the pyridoxal 5'-phosphate cofactor and a second domain primarily composed of beta-strands. The cofactor adopts two partially occupied conformational states that resemble previously reported and external aldimine complexes
pyridoxal 5'-phosphate
-
enzyme is dependent on, maximal activity at 0.025 mM
pyridoxal 5'-phosphate
-
Km at 30°C is 0.005 mM. Maximal activity is obtained in presence of more than 0.125 mM pyridoxal 5'-phosphate. The decrease in activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
Km: 0.005 mM, at 30°C
pyridoxal 5'-phosphate
-
the pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
pyridoxal 5'-phosphate
covalently linked to enzyme at K42
pyridoxal 5'-phosphate
Q81VF6
C-terminal region of 1 subdomain: Arg138 donates a hydrogen bond to the phenolic O atom of PLP, Arg224 donates a hydrogen bond to the pyridinyl N atom of PLP, Lys41 forms an aldimine linkage with the PLP, eliminating water to form the Schiff base, C-terminal atoms of second subunit Ser209, Gly226 and Ile227 stabilize the PLP phosphate with the help of Ser209 O(gamma), Tyr45 O(eta) and Tyr359 O(eta)
pyridoxal 5'-phosphate
once per 1 million turnovers of racemization a H-atom is added to C4-atom of the substrate moiety of the anionic intermediate instead of the reprotonation of the abstracted hydrogen at C(alpha) resulting in pyridoxamine 5'-phosphate
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
pyridoxal 5'-phosphate
Alkalihalophilus pseudofirmus
PLP is bound to the enzyme, adding PLP during developement of enzyme or to an assay is not necessary
pyridoxal 5'-phosphate
-
PLP is inherently bound to the enzyme, removal of PLP inactivates the enzyme, adding PLP restores the activity, addition of 10 microM PLP to native enzyme slightly enhances activity
pyridoxal 5'-phosphate
dependent on, alanine racemase requires pyridoxal-5'-phosphate as a cofactor to form a Schiff base between pyridoxal 5'-phosphate and epsilon-amino group of the lysine residue in the active site
pyridoxal 5'-phosphate
dependent on, pyridoxal 5'-phosphate is bound to each monomer of the dimeric enzyme and forms a Schiff base with Lys39
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
-
PLP, dependent on
pyridoxal 5'-phosphate
Alkalihalophilus pseudofirmus
PLP, dependent on
pyridoxal 5'-phosphate
PLP, dependent on
pyridoxal 5'-phosphate
PLP, dependent on
pyridoxal 5'-phosphate
PLP, dependent on, binding structure analysis: the phosphate group of the pyridoxal 5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240. The pyridine ring of the PLP is stabilized by a hydrogen bond between the N-1 of the cofactor and Nepsilon of Arg237. The C2A of the PLP also interacts with oxygen Q1 of the carboxylated Lys141. All residues stabilizing the PLP cofactor (Tyr50, Ser222, Gly239, Ile240, Arg237, Tyr374) are conserved among Alr proteins. But the AlrSco lacks one important hydrogen bond between Arg148 and the phenolic oxygen of the PLP molecule
pyridoxal 5'-phosphate
-
PLP, dependent on, enzyme-cofactor complex structure, with inhibitor acetate, PDB ID 1SFT
pyridoxal 5'-phosphate
PLP, dependent on, no catalytic enzyme activity without, the apoenzyme activity is completely inhibited
pyridoxal 5'-phosphate
PLP, dependent on. The PLP-binding motif containing the catalytic Lys34 (sequence SMVKANAYGHG) is largely conserved between the various enzymes. The essential PLP cofactor is covalently bound to Lys34 via an internal aldimine linkage and extends towards the centre of the alpha/beta-barrel. The pyridine N1 of the PLP ring is stabilized by hydrogen bonding to Arg209, which is further stabilized by interactions with His159. The phosphate tail of PLP is stabilized by several residues from one monomer. The OP1 of the phosphate group hydrogen bonds to Ile212 and Tyr38, OP2 hydrogen bonds to Try341 and OP3 hydrogen bonds to Ile212 and Ser190. Arg132 is not within hydrogen-bonding distance of PLP in the AlrAba structure
pyridoxal 5'-phosphate
PLP, the PLP content of the enzyme is determined by a spectroscopic method
additional information
-
contains a pyridoxal 5'-phosphate binding site
-
additional information
-
exogenous pyridoxal 5-phosphate is not required, but enzyme may be pyridoxal 5-phosphate-dependent
-
additional information
-
not activated by pyridoxal 5'-phosphate
-
additional information
there is no additional density in the AlrAba structure consistent with the presence of any additional ligands besides pyridoxal 5'-phosphate
-
additional information
-
there is no additional density in the AlrAba structure consistent with the presence of any additional ligands besides pyridoxal 5'-phosphate
-
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((6R)-2-carboxy-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl)methyl 3-chloro-D-alanyl-D-alaninate
-
(1-aminoethyl)boronic acid
(1-Aminoethyl)phosphonate
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
(2S)-1-oxo-1-[[(1R)-1-phosphonoethyl]amino]propan-2-yl L-methioninate
(4R)-4-amino-3-isoxazolidinone
-
-
(6R)-3-[(D-alanyloxy)methyl]-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
(R)-1-aminoethylphosphonic acid
1,1'-(2-oxido-1,2,5-oxadiazole-3,4-diyl)-bis (1-(2-thienyl))-methanone
-
-
1,2,4-thiadiazolidine-3,5-dione
-
-
1-amino-cyclopropane phosphonate
-
-
2-(2-chloro-4-nitrophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
2-(2-chloro-4-nitrophenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
2-(2-chloro-6-methylphenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
2-(2-hydroxyphenoxy)-N-methylacetamide
-
-
2-(3,5-dimethyl-1,2-oxazol-4-yl)-4-(4-fluorophenyl)-1,2,4-thiadiazolidine-3,5-dione
2-(3-chloro-4-fluorophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
2-(4,6-dimethyl-3-oxo-[1,2]thiazolo[5,4-b]pyridin-2-yl)-N-[2-(4-ethoxyphenyl)ethyl]acetamide
-
-
2-(4-methoxyphenyl)-1-morpholin-4-ylethanethione
-
-
2-(4-methylphenyl)-1-morpholin-4-ylethanethione
-
-
2-(9-acridinylamino)benzenepropanoic acid
-
2-(hydoxyimino)-6-methyl-2H-benzopyran-3-carboxamide
-
-
2-(pyridin-3-ylcarbamothioyl sulfanyl)acetic acid
-
-
2-Amino-3-chlorobut-3-enoic acid
2-Amino-3-fluorobut-3-enoic acid
2-N',2-N',7-N',7-N'-tetramethyl-9H-fluorene-2,7-disulfonohydrazide
-
-
2-phenyl-1-piperidin-1-ylethanethione
-
-
3,3-dihydroxy-1H-quinoline-2,4-dione
-
-
4-(2,3-dihydro-1H-inden-2-yl)-2-[(3-ethylphenyl)methyl]-1,2,4-thiadiazolidine-3,5-dione
4-(cyclopropylmethyl)-2-(3,5-dimethyl-1,2-oxazol-4-yl)-1,2,4-thiadiazolidine-3,5-dione
4-(cyclopropylmethyl)-2-[2-(trifluoromethyl)phenyl]-1,2,4-thiadiazolidine-3,5-dione
4-methyl-2-(naphthalen-1-yl)-1,2,4-thiadiazolidine-3,5-dione
4-methyl-2-phenyl-1,2,4-thiadiazolidine-3,5-dione
4-[4-(propan-2-yl)phenyl]-2-[4-[(trifluoromethyl)sulfanyl]phenyl]-1,2,4-thiadiazolidine-3,5-dione
5-chloro-N-(3-chloro-4-methoxyphenyl)-2-(methylsulfonyl)pyrimidine-4-carboxamide
-
-
6-O-[3-chloro-4-(6-methoxycarbonylpyridine-2-carbonyl)oxyphenyl] 2-O-methyl pyridine-2,6-dicarboxylate
-
-
Aminooxyacetate
-
1 mM, complete inhibition, both directions
beta,beta,beta-trifluoroalanine
Cu2+
-
40% residual activity at 1 mM
D-penicillamine
-
1 mM, 79% inhibition
DTT
DTT at 1 mmol/l inhibits 67% of the enzyme activity compared with the control and DTT at 5 mmol/l results in complete inhibition of the enzyme activity
ethyl 3-(pyridin-2-ylthio)propanoate
-
-
FAD
-
slight activation at low concentrations, inhibition at high concentrations
homogentisic acid
competitive inhibition, has minimal cytotoxicity against mammalian cells. Homogentisic acid binds to the active site of the racemase
hydroquinone
noncompetitive inhibition, has minimal cytotoxicity against mammalian cells. Hydroquinone binds near the active center of alanine racemase
L-alanine phosphonic acid
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
L-norvalyl-L-chlorovinylglycine
L-Penicillamine
-
1 mM, 28% inhibition
N',N',4-trimethylbenzenesulfonohydrazide
-
-
N-benzyl-5-chloro-2-methylsulfonylpyrimidine-4-carboxamide
-
-
N-hydroxy-2-(2-hydroxyphenoxy)acetamide
-
-
N2-(2-aminodecanoyl)-N-[(1R)-1-phosphonoethyl]-L-alaninamide
NaBH4
-
0.5 M, loss of activity
NEM
-
1 mM, 22% inhibition
norleucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
norvalyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
O-acetyl-D-serine
-
reversible inhibitor
O-Carbamoyl-D-Ser
-
inhibition of wild type enzyme but not of the O-carbamoyl-D-Ser mutant
PCMB
-
1 mM, 91% inhibition
[(1R)-1-amino-2-chloroethyl]phosphonic acid
-
[4-(5-butyl-5-methyl-2(5H)-furanylidene)dihydro-3,5-dioxo-2(3H)-furanylidene]acetic acid
-
(1-aminoethyl)boronic acid
-
-
(1-aminoethyl)boronic acid
-
-
(1-aminoethyl)boronic acid
-
Ala-B
(1-Aminoethyl)phosphonate
-
D- and L-(1-aminoethyl)phosphonate
(1-Aminoethyl)phosphonate
-
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
-
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
-
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
-
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
-
-
(2S)-1-oxo-1-[[(1R)-1-phosphonoethyl]amino]propan-2-yl L-methioninate
-
-
(2S)-1-oxo-1-[[(1R)-1-phosphonoethyl]amino]propan-2-yl L-methioninate
-
-
(6R)-3-[(D-alanyloxy)methyl]-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
(6R)-3-[(D-alanyloxy)methyl]-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
(6R)-3-[(D-alanyloxy)methyl]-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
(6R)-3-[(D-alanyloxy)methyl]-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
(R)-1-aminoethylphosphonic acid
Q81VF6
in combination with pyridoxal 5'-phosphate
(R)-1-aminoethylphosphonic acid
upon formation of the external aldimine the phosphonate group interacts with putative catalytic residues, thereby rendering them unavailable for catalysis
2-(2-chloro-4-nitrophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(2-chloro-4-nitrophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(2-chloro-4-nitrophenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(2-chloro-4-nitrophenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(2-chloro-6-methylphenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(2-chloro-6-methylphenyl)-4-(cyclopropylmethyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(3,5-dimethyl-1,2-oxazol-4-yl)-4-(4-fluorophenyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(3,5-dimethyl-1,2-oxazol-4-yl)-4-(4-fluorophenyl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(3-chloro-4-fluorophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-(3-chloro-4-fluorophenyl)-4-(2,3-dihydro-1H-inden-2-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
2-Amino-3-chlorobut-3-enoic acid
-
i.e. 3-chlorovinylglycine, irreversible
2-Amino-3-chlorobut-3-enoic acid
-
-
2-Amino-3-fluorobut-3-enoic acid
-
i.e. 3-fluorovinylglycine, irreversible
2-Amino-3-fluorobut-3-enoic acid
-
-
4-(2,3-dihydro-1H-inden-2-yl)-2-[(3-ethylphenyl)methyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
4-(2,3-dihydro-1H-inden-2-yl)-2-[(3-ethylphenyl)methyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
4-(cyclopropylmethyl)-2-(3,5-dimethyl-1,2-oxazol-4-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
4-(cyclopropylmethyl)-2-(3,5-dimethyl-1,2-oxazol-4-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
4-(cyclopropylmethyl)-2-[2-(trifluoromethyl)phenyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
4-(cyclopropylmethyl)-2-[2-(trifluoromethyl)phenyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
4-methyl-2-(naphthalen-1-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
4-methyl-2-(naphthalen-1-yl)-1,2,4-thiadiazolidine-3,5-dione
-
-
4-methyl-2-phenyl-1,2,4-thiadiazolidine-3,5-dione
-
-
4-methyl-2-phenyl-1,2,4-thiadiazolidine-3,5-dione
-
-
4-[4-(propan-2-yl)phenyl]-2-[4-[(trifluoromethyl)sulfanyl]phenyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
4-[4-(propan-2-yl)phenyl]-2-[4-[(trifluoromethyl)sulfanyl]phenyl]-1,2,4-thiadiazolidine-3,5-dione
-
-
acetate
-
acetate
-
enzyme-inhibitor complex structure, with pyridoxyl 5'-phosphate, PDB ID 1SFT
alafosfalin
-
-
alafosfalin
-
effective in reducing D-alanine pool levels, alafosfalin forms an external aldimine with the bound PLP cofactor, but is neither racemised nor efficiently hydrolyzed and upon formation of the external aldimine, the phosphonate group interacts with putative catalytic residues and thereby renders them unavailable for catalysis
alafosfalin
selective inhibitor of peptidoglycan biosynthesis in both Grampositive and Gram-negative bacteria
alafosfalin
-
effective in reducing D-alanine pool levels, alafosfalin forms an external aldimine with the bound PLP cofactor, but is neither racemised nor efficiently hydrolyzed and upon formation of the external aldimine, the phosphonate group interacted with putative catalytic residues and thereby renders them unavailable for catalysis
aminooxyacetic acid
-
-
aminooxyacetic acid
-
1 mM, complete inhibition
beta,beta,beta-trifluoroalanine
-
nucleophilic attack of Lys38 on the electrophilic beta-difluoro-alpha,beta-unsaturated imine
beta,beta,beta-trifluoroalanine
-
-
beta,beta,beta-trifluoroalanine
-
nucleophilic attack of Lys38 on the electrophilic beta-difluoro-alpha,beta-unsaturated imine
beta-Chloro-D-alanine
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. Glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase and is therefore unable to undergo the same mechanism of inhibition as Alr with BCDA
beta-Chloro-D-alanine
90-95% inhibition
beta-Chloro-D-alanine
BCDA, the compund is a very poor inhibitor of recombinant Mycobacterium tuberculosis Alr, despite having potent antituberculosis activity, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. Glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase and is therefore unable to undergo the same mechanism of inhibition as Alr with BCDA
beta-Chloro-D-alanine
90-95% inhibition
beta-Chloro-D-alanine
-
effective in the inhibition of bacterial growth
beta-chloro-L-alanine
-
beta-chloro-L-alanine
-
effective in the inhibition of bacterial growth like that of the D-isomer. But the L-isomer has less specificity towards the concerned Alr enzymes due to its inhibitory activity towards decarboxylase and transaminases. This results in the blockage of the production of essential L-amino acids with a loss of viability of bacterial and mammalial cells
beta-chloroalanine
-
enantiomers of beta-chloroalanine as Alr inhibitors
chlorovinyl glycine
-
-
chlorovinylglycine
-
-
cycloserine
-
8 microg/ml bacterial culture extract markedly inhibits alanine racemase
cycloserine
suicide inhibitor
cycloserine
-
D-cycloserine or a racemic mixture of D- and L-cycloserine
cycloserine
D-cycloserine or a racemic mixture of D- and L-cycloserine
D-Chloroalanine
-
Ki: 0.005 mM, competitive
D-cycloserine
-
D-cycloserine
-
an alanine racemase inhibitor
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
active site bound inhibitor, binding structure, overview
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
-
time-dependent inactivation rate of enzyme from Streptomyces lavendulae is slower than for enzyme from Escherichia coli
D-cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
specific inhibition is reversible by D-alanine in the growth medium
D-cycloserine
-
DCS, inhibits enzyme Alr irreversibly by covalently bonding to pyridoxal 5'-phosphate, molecular modeling
D-cycloserine
-
1 mM, 95% inhibition
D-cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
-
competitive inhibitor, importance of N2-structural site in cyloserine for bioactivity
D-cycloserine
structural features such as the hinge angle or the surface area between the monomers do not contribute to D-cycloserine resistance, binding structure analysis, overview
D-cycloserine
time-dependent inactivation rate of enzyme from Streptomyces lavendulae is slower than for enzyme from Escherichia coli. Enzyme from Streptomyces lavendulae is one of its self-resistance determinants
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
hydroxylamine
-
1 mM, 68% inhibition
hydroxylamine
via elimanting the cofactor pyridoxal-5'-phosphate from the enzyme
hydroxylamine
-
non-competitive inhibition kinetics
hydroxylamine
-
1 mM, complete inhibition, both directions
hydroxylamine
-
1 mM, complete inhibition
L-chloroalanine
-
Ki: 1.71 mM, noncompetitive
L-Cycloserine
-
-
L-Cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
L-Cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
-
1 mM, 90% inhibition
L-Cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
-
competitive inhibitor, importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-leucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
L-norvalyl-L-chlorovinylglycine
-
-
L-norvalyl-L-chlorovinylglycine
-
-
L-norvalyl-L-chlorovinylglycine
-
-
L-norvalyl-L-chlorovinylglycine
-
L-norvalyl-L-chlorovinylglycine
-
-
N2-(2-aminodecanoyl)-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
N2-(2-aminodecanoyl)-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
N2-(2-aminodecanoyl)-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
NaCl
-
slight inhibition above 600 mM
NaCl
-
at concentrations around seawater level
norleucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
moderate in vivo activity
norleucyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
norvalyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
moderate in vivo activity
norvalyl-N-[(1R)-1-phosphonoethyl]-L-alaninamide
-
-
O-carbamoyl-D-serine
-
-
O-carbamoyl-D-serine
-
good inhibitor, determination of primary site of action is based on the observed accumulation of UDP-MurNAc-L-Ala-D-Glu-L-Lys and on the absence of D-Ala-O-carbamyl-D-serine accumulation
phenylhydrazine
-
-
phenylhydrazine
-
1 mM, 72% inhibition
propionate
-
propionate influences both Km (affinity for substrate) and Vmax (enzyme catalysis)
propionate
binding structure analysis, overview
pyridoxal 5'-phosphate
-
slight activation at low concentrations, inhibition at high concentrations
pyridoxal 5'-phosphate
-
0.4 mM, 51% inhibition
pyruvate
-
Sodium borohydride
-
1 mM, 30% inhibition
Sodium borohydride
complete inactivation after dialysis against
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
additional information
inhibitor screening of a library of 2100 compounds, and molecular docking study
-
additional information
the enzyme activity is not sensitive to the metal chelating agent EDTA indicating that divalent cations are not required for enzyme activity
-
additional information
-
structure-based inhibitor design
-
additional information
-
no inhibition by O-carbamoyl-L-serine
-
additional information
-
no inhibition by O-carbamoyl-L-serine
-
additional information
wild-type enzyme ALR is strongly activated by low concentrations (e.g. 1 mM) of short-chain carboxylates, and is inhibited at higher concentrations (e.g. 10 mM). The enzyme mutant ALRA131K is inhibited at all carboxylate concentrations tested (1-40 mM). Both propionate and butyrate strongly inhibit mutant ALRA131K. ALR and ALRA131K are both inhibited by DL-lactate, though wild-type ALR is inhibited to a lesser degree than ALRA131K. In addition, succinate, pyruvate, 2-oxoglutarate, oxaloacetate, and aspartate also more strongly inhibit mutant ALRA131K than wild-type ALR
-
additional information
-
wild-type enzyme ALR is strongly activated by low concentrations (e.g. 1 mM) of short-chain carboxylates, and is inhibited at higher concentrations (e.g. 10 mM). The enzyme mutant ALRA131K is inhibited at all carboxylate concentrations tested (1-40 mM). Both propionate and butyrate strongly inhibit mutant ALRA131K. ALR and ALRA131K are both inhibited by DL-lactate, though wild-type ALR is inhibited to a lesser degree than ALRA131K. In addition, succinate, pyruvate, 2-oxoglutarate, oxaloacetate, and aspartate also more strongly inhibit mutant ALRA131K than wild-type ALR
-
additional information
-
N2-substitution of carboxybenzyl-protected derivatives of D,L-cycloserine proceed smoothly with the requisite alkyl halide in the presence of potassium tert-butoxide in dimethylformamide. The synthesised compounds are evaluated for their inhibitory activity against purified Alrs (Alr gene product). Structural modification at the N2 position result in reduced activity in the enzyme assay and underscore the importance of structural modification at N2-position of cycloserine. A compound with CH2CONHOCH3 substituent at N2 position exhibits modest inhibitory activity against purified Alr enzyme from Mycobacterium tuberculosis, Ki = 0.36 mM
-
additional information
N2-substitution of carboxybenzyl-protected derivatives of DL-cycloserine proceed smoothly with the requisite alkyl halide in the presence of potassium tert-butoxide in dimethylformamide. The synthesised compounds are evaluated for their inhibitory activity against purified Alrs (Alr gene product). Structural modification at the N2 position result in reduced activity in the enzyme assay and underscore the importance of structural modification at N2-position of cycloserine. A compound with CH2CONHOCH3 substituent at (N)-2 position exhibits modest inhibitory activity against purified Alr enzyme from Escherichia coli, Ki is 0.47 mM. No inhibition by ((6R)-2-carboxy-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl)methyl 3-chloro-D-alanyl-3-chloro-D-alaninate
-
additional information
the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design, formation of a template for structure-based drug-development efforts targeting the enzyme, overview
-
additional information
-
the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design, formation of a template for structure-based drug-development efforts targeting the enzyme, overview
-
additional information
-
no inhibition by O-carbamoyl-L-serine. N2-substitution of carboxybenzyl-protected derivatives of D,L-cycloserine proceed smoothly with the requisite alkyl halide in the presence of potassium tert-butoxide in dimethylformamide. The synthesised compounds are evaluated for their inhibitory activity against purified Alrs (Alr gene product). Structural modification at the N2 position result in reduced activity in the enzyme assay and underscore the importance of structural modification at N2-position of cycloserine. A compound with CH2CONHOCH3 substituent at (N)-2 position exhibits modest inhibitory activity against purified Alr enzyme from Streptococcus aureus, Ki = 1.16 mM
-
additional information
not inhibitory: L-cycloserine
-
additional information
-
not inhibitory: L-cycloserine
-
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18
D-Lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
10
D-serine
-
pH 8.2, 37°C
32
L-lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
27
L-serine
-
pH 8.2, 37°C
additional information
additional information
-
0.4
D-Ala
-
-
0.5
D-Ala
-
alr gene encoded
1.1
D-Ala
-
23°C, enzyme Alr
1.4
D-Ala
-
23°C, enzyme DadX
2.2
D-Ala
-
D-Ala, dadB encoded enzyme
73.5
D-Ala
-
30°C, pH 8.5
0.25
D-alanine
-
pH 8.2, 37°C
0.304
D-alanine
+/-0.034, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.311
D-alanine
+/-0.008, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.4
D-alanine
-
pH 8.2, 37°C
0.402
D-alanine
+/-0.055, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.439
D-alanine
+/-0.080, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.46
D-alanine
-
pH and temperature not specified in the publication
0.48
D-alanine
-
pH and temperature not specified in the publication
0.513
D-alanine
+/-0.084, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.528
D-alanine
+/-0.079, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.56
D-alanine
pH not specified in the publication, 30°C
0.592
D-alanine
+/-0.085, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.604
D-alanine
+/-0.070, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.615
D-alanine
+/-0.032, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
0.7
D-alanine
pH 8.2, 25°C
0.89
D-alanine
pH not specified in the publication, 30°C, recombinant enzyme
1.008
D-alanine
+/-0.069, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.4
D-alanine
-
pH 7.6, 37°C, recombinant enzyme
2.3
D-alanine
pH 8.0, 30°C, recombinant mutant Y354W
2.6
D-alanine
pH 8.0, 30°C, recombinant mutant I222T
2.8
D-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
4
D-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
4.2
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
4.7
D-alanine
-
pH 7.4, 30°C
4.7
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
5.4
D-alanine
pH 8.5, temperature not specified in the publication, recombinant mutant K271T
5.6
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
6.1
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
6.2
D-alanine
Vmax 37.9 micromol/min/mg
6.9
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
7
D-alanine
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
7.3
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.7
D-alanine
-
pH 7.4, 30°C
8.7
D-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
12
D-alanine
-
Vmax = 0.44 mol/s/kg
14.91
D-alanine
Alkalihalophilus pseudofirmus
-
15.36
D-alanine
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
20.16
D-alanine
pH 11.0, 70°C, recombinant enzyme
20.4
D-alanine
-
HPLC analysis
20.78
D-alanine
Alkalihalophilus pseudofirmus
pH 10.5, 40°C, recombinant wild-type enzyme
52
D-alanine
pH 10.0, 65°C, recombinant mutant Q360Y
58.5
D-alanine
pH 10.0, 65°C, recombinant mutant S173D/Q360Y
110.3
D-alanine
pH 10.0, 65°C, recombinant mutant Q360I
160.9
D-alanine
pH 10.0, 65°C, recombinant mutant S173D
216.1
D-alanine
pH 10.0, 65°C, recombinant mutant Q360W
381.2
D-alanine
pH 10.0, 65°C, recombinant wild-type enzyme
0.5
L-Ala
-
-
1.1
L-Ala
-
23°C, enzyme Alr
1.4
L-Ala
-
23°C, enzyme DadX
1.7
L-Ala
-
alr gene encoded
11
L-Ala
-
dadB gene encoded
0.046
L-alanine
pH 7.5, 37°C, recombinant mutant K39A
0.064
L-alanine
pH 7.5, 37°C, recombinant wild-type enzyme
0.29
L-alanine
-
pH 8.2, 37°C
0.38
L-alanine
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
0.4
L-alanine
-
pH 8.2, 37°C
0.7
L-alanine
pH 8.2, 25°C
0.97
L-alanine
-
pH and temperature not specified in the publication
1.049
L-alanine
+/-0.131, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.401
L-alanine
+/-0.209, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.516
L-alanine
+/-0.083, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.562
L-alanine
+/-0.256, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.993
L-alanine
+/-0.269, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2.057
L-alanine
+/-0.038, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2.77
L-alanine
pH not specified in the publication, 30°C, recombinant enzyme
3.03
L-alanine
+/-0.114, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
3.603
L-alanine
+/-0.180, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
3.7
L-alanine
pH 7.6, 37°C
3.8
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C
4.1
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
4.2
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer
4.5
L-alanine
pH 8.0, 30°C, recombinant mutant Y354W
4.7
L-alanine
pH 8.0, 30°C, recombinant mutant I222T
4.8
L-alanine
-
pH 7.6, 37°C, recombinant enzyme
5.1
L-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
5.9
L-alanine
pH 7.6, 37°C
6.8
L-alanine
-
pH and temperature not specified in the publication
7.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.1
L-alanine
-
pH 7.4, 30°C
8.1
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
8.2
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
8.3
L-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
9.3
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
9.8
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
10.34
L-alanine
-
at pH 9.0 and 37°C
12
L-alanine
recombinant MBP-tagged enzyme, pH 8.0, 37°C
13.8
L-alanine
pH 8.5, temperature not specified in the publication, recombinant mutant K271T
17.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
17.6
L-alanine
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
18.4
L-alanine
-
pH 7.4, 30°C
18.4
L-alanine
-
in 50 mM potassium phosphate buffer pH 7.4, at 30°C
29.6
L-alanine
-
Vmax = 1.02 mol/s/kg
35.9
L-alanine
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
41.79
L-alanine
Alkalihalophilus pseudofirmus
-
43
L-alanine
-
HPLC analysis
56.17
L-alanine
Alkalihalophilus pseudofirmus
pH 10.5, 40°C, recombinant wild-type enzyme
83.1
L-alanine
pH 10.0, 65°C, recombinant mutant S173D/Q360Y
87.8
L-alanine
pH 10.0, 65°C, recombinant mutant Q360Y
100
L-alanine
Vmax 909 micromol/min/mg
136
L-alanine
pH 10.0, 65°C, recombinant mutant Q360I
157.5
L-alanine
pH 10.0, 65°C, recombinant mutant S173D
176.1
L-alanine
pH 10.0, 65°C, recombinant mutant Q360W
780.2
L-alanine
pH 10.0, 65°C, recombinant wild-type enzyme
additional information
additional information
-
Km values of L-Ala in the presence of urea at various concentrations
-
additional information
additional information
-
Km values of L-Ala in the presence of urea at various concentrations
-
additional information
additional information
-
effect of NaCl on Km-value
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Vmax 110 micromol/min/mg D-alanine
-
additional information
additional information
-
Vmax 306 U/mg: D-alanine to L-alanine
-
additional information
additional information
-
Vmax 323 micromol/min/mg L-alanine
-
additional information
additional information
-
Vmax 345 U/mg: L-alanine to D-alanine
-
additional information
additional information
Vmax for the racemization (D- to L-alanine and L- to D-alanine) is 87.0 and 84.8 U/mg, respectively.
-
additional information
additional information
-
Vmax for the racemization (D- to L-alanine and L- to D-alanine) is 87.0 and 84.8 U/mg, respectively.
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
Alkalihalophilus pseudofirmus
enzyme kinetics analysis
-
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2.5
D-Lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
5.5
D-serine
-
pH 8.2, 37°C
0.0024 - 3275.5
L-alanine
4.17
L-lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
13.3
L-serine
-
pH 8.2, 37°C
1.6
D-Ala
-
dadB encoded enzyme
2.6
D-Ala
-
alr encoded enzyme
24.8
D-Ala
-
90°C, pH 9.5
2314
D-Ala
-
pH 8.5, 37°C
3270
D-Ala
-
30°C, pH 8.5
3272
D-Ala
-
30°C, pH 8.5
0.06
D-alanine
-
pH 7.6, 37°C, recombinant enzyme
0.333
D-alanine
+/-0.033, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
1.317
D-alanine
+/-0.100, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
2 - 8
D-alanine
-
pH 8.2, 37°C
4
D-alanine
+/-0.417, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
4.466
D-alanine
+/-0.200, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
5.267
D-alanine
+/-0.333, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
5.783
D-alanine
+/-0.483, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
6.35
D-alanine
+/-0.333, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
6.817
D-alanine
+/-0.650, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
7.617
D-alanine
+/-0.750, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
19.25
D-alanine
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
32.5
D-alanine
pH 10.0, 65°C, recombinant mutant S173D
63.3
D-alanine
-
pH 8.2, 37°C
70
D-alanine
pH 8.2, 25°C
96.9
D-alanine
pH 10.0, 65°C, recombinant wild-type enzyme
133.1
D-alanine
pH 10.0, 65°C, recombinant mutant S173D/Q360Y
225
D-alanine
pH 10.0, 65°C, recombinant mutant Q360I
251.2
D-alanine
pH 10.0, 65°C, recombinant mutant Q360Y
517
D-alanine
pH 8.0, 30°C, recombinant mutant Y354W
633
D-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
633.5
D-alanine
pH 10.0, 65°C, recombinant mutant Q360W
983
D-alanine
pH 8.0, 30°C, recombinant mutant I222T
1017
D-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
1298.4
D-alanine
pH 8.5, temperature not specified in the publication, recombinant mutant K271T
1.1
L-Ala
-
-
7.3
L-Ala
-
dadB encoded enzyme
9.7
L-Ala
-
alr encoded enzyme
2589
L-Ala
-
pH 8.5, 37°C
7500
L-Ala
-
30°C, pH 8.5
7504
L-Ala
-
30°C, pH 8.5
0.0024
L-alanine
recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer
0.0065
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer
0.022
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer
0.15
L-alanine
recombinant MBP-tagged enzyme, pH 8.0, 37°C
0.9
L-alanine
-
pH 7.6, 37°C, recombinant enzyme
2.3
L-alanine
recombinant His-tagged enzyme, pH 8.0, 37°C
2.8
L-alanine
+/-0.250, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
16.72
L-alanine
+/-0.850, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
22.47
L-alanine
+/-2.667, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
27.6
L-alanine
-
pH 8.2, 37°C
34.7
L-alanine
pH 10.0, 65°C, recombinant mutant S173D
37
L-alanine
pH 7.6, 37°C
41.82
L-alanine
+/-2.600, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
51.77
L-alanine
+/-6.067, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
53.98
L-alanine
+/-3.217, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
55
L-alanine
pH 8.2, 25°C
55
L-alanine
-
pH 8.2, 37°C
59.3
L-alanine
pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme
67.07
L-alanine
+/-7.633, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
68.23
L-alanine
+/-7.550, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
70.63
L-alanine
-
at pH 9.0 and 37°C
70.92
L-alanine
+/-2.333, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm
212.4
L-alanine
pH 10.0, 65°C, recombinant wild-type enzyme
246.5
L-alanine
pH 10.0, 65°C, recombinant mutant S173D/Q360Y
286.6
L-alanine
pH 10.0, 65°C, recombinant mutant Q360I
431.5
L-alanine
pH 10.0, 65°C, recombinant mutant Q360Y
612.4
L-alanine
pH 10.0, 65°C, recombinant mutant Q360W
1133
L-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
1133
L-alanine
pH 8.0, 30°C, recombinant mutant Y354W
1190
L-alanine
pH 7.6, 37°C
1417
L-alanine
pH 8.0, 30°C, recombinant mutant I222T
1533
L-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
3275.5
L-alanine
pH 8.5, temperature not specified in the publication, recombinant mutant K271T
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0.058
(4R)-4-amino-3-isoxazolidinone
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0049
1,1'-(2-oxido-1,2,5-oxadiazole-3,4-diyl)-bis (1-(2-thienyl))-methanone
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0057
2-(2-hydroxyphenoxy)-N-methylacetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0077
2-(4,6-dimethyl-3-oxo-[1,2]thiazolo[5,4-b]pyridin-2-yl)-N-[2-(4-ethoxyphenyl)ethyl]acetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0033
2-(4-methoxyphenyl)-1-morpholin-4-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0065
2-(4-methylphenyl)-1-morpholin-4-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0177
2-(9-acridinylamino)benzenepropanoic acid
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0028
2-(hydoxyimino)-6-methyl-2H-benzopyran-3-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0131
2-(pyridin-3-ylcarbamothioyl sulfanyl)acetic acid
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0016
2-N',2-N',7-N',7-N'-tetramethyl-9H-fluorene-2,7-disulfonohydrazide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.006
2-phenyl-1-piperidin-1-ylethanethione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0052
3,3-dihydroxy-1H-quinoline-2,4-dione
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0082
5-chloro-N-(3-chloro-4-methoxyphenyl)-2-(methylsulfonyl)pyrimidine-4-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.001
6-O-[3-chloro-4-(6-methoxycarbonylpyridine-2-carbonyl)oxyphenyl] 2-O-methyl pyridine-2,6-dicarboxylate
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0066
anabellamide
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0054 - 1.328
D-cycloserine
0.0026
ethyl 3-(pyridin-2-ylthio)propanoate
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0156
hematoxylin
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0143
higenamine
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0125
homogentisic acid
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0185
hydroquinone
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
2.1
L-Cycloserine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.009
N',N',4-trimethylbenzenesulfonohydrazide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0068
N-benzyl-5-chloro-2-methylsulfonylpyrimidine-4-carboxamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0082
N-hydroxy-2-(2-hydroxyphenoxy)acetamide
Mycobacterium tuberculosis
-
in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication
0.0147
patulin
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0086
propyl gallate
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0155
quercetin
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0089
[4-(5-butyl-5-methyl-2(5H)-furanylidene)dihydro-3,5-dioxo-2(3H)-furanylidene]acetic acid
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0054
D-cycloserine
Aeromonas hydrophila subsp. hydrophila
pH 11.0, 35°C, recombinant His-tagged enzyme
0.0264
D-cycloserine
Mycobacterium tuberculosis
-
wild-type enzyme, pH and temperature not specified in the publication
0.65
D-cycloserine
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.712
D-cycloserine
Mycobacterium tuberculosis
-
enzyme mutant R373L, pH and temperature not specified in the publication
1.328
D-cycloserine
Mycobacterium tuberculosis
-
enzyme mutant Y364D, pH and temperature not specified in the publication
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evolution
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
-
the enzyme shows evolutionary and structural similarity to the promiscuous enzymes serine hydroxymethyltransferase, EC 2.1.2.1, and threonine aldolase, EC 4.1.2.48. The three enzymes represent a model of divergent evolution from an ancestral enzyme that was able to catalyse all the reactions of the modern enzymes. Similarly to serine hydroxymethyltransferase and threonine aldolase, Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. The genome sequences of methanogenic archaeon, Methanococcus maripaludis reveals the presence of alanine dehydrogenase gene adjacent to genes for alanine racemase and alanine permease, apparently acquired from bacteria
evolution
-
alanine racemase is a fold type III pyridoxal-5'-phosphate-dependent amino acid racemase enzyme
evolution
in bacteria, two types of alanine racemase are encoded independently by two genes named dadX and alr. The dadX gene encodes a catabolic alanine racemase DadX, which catalyzes direct conversion of L-Ala to D-Ala. Its expression is induced by L- or D-Ala. The alr gene encodes an anabolic alanine racemase Alr, it is expressed constitutively at low level and essential for providing abundant D-Ala for peptidoglycan biosynthesis. Some bacteria only contain one type alanine racemase gene, whereas others have two of them. Thermoanaerobacter tengcongensis strain MB4 contains two annotated alanine racemase genes MBalr1 and MBalr2. Both genes encode 388 amino acids long alanine racemase, sharing a 58.3% amino acid sequence identity. Compared with MBAlr2, MBAlr1 shows very low catalytic efficiency and limited substrate spectrum. It is probable that MBAlr1 serves as an anabolic and MBAlr2 as the catabolic alanine racemase in Thermoanaerobacter tengcongensis strain MB4
evolution
the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes
evolution
two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes
-
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes
-
evolution
-
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
malfunction
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
malfunction
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
malfunction
because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
malfunction
depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
malfunction
depletion of alr in Streptococcus mutans significantly compromises its competitiveness with other co-residents, e.g. Streptococcus sanguinis, in the oral biofilm. D-Ala starvation causes cell morphology alterations of the alr mutant
malfunction
Alkalihalophilus pseudofirmus
enzyme Alr inhibition is lethal to prokaryotes
malfunction
-
growth of the Alr mutant on a mixture of D- and L-alanine is compromised
malfunction
inhibition of the enzyme is lethal to prokaryotes
malfunction
lack of expression of the alr gene is lethal when there is no addition of exogenous D-Ala. Upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Decreased cariogenicity of alr-mutant strain in rats
malfunction
Mycobacterium smegmatis strains with a deletion of the alr gene require D-Ala for growth, indicating the essential role of Alr in D-Ala production. Gln360 and conformational changes of active site residues disrupt the hydrogen bonding interactions necessary for proper pyridoxal 5'-phosphate immobilization, and decrease both the substrate affinity and turnover number of AlrTt. Introduction of hydrophobic amino acids at Gln360 increase the racemase activity of AlrTt
malfunction
-
role of alanine racemase mutations in Mycobacterium tuberculosis D-cycloserine resistance, overview
malfunction
-
depletion of alr in Streptococcus mutans significantly compromises its competitiveness with other co-residents, e.g. Streptococcus sanguinis, in the oral biofilm. D-Ala starvation causes cell morphology alterations of the alr mutant
-
malfunction
-
lack of expression of the alr gene is lethal when there is no addition of exogenous D-Ala. Upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Decreased cariogenicity of alr-mutant strain in rats
-
malfunction
-
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
-
malfunction
Alkalihalophilus pseudofirmus OF4
-
enzyme Alr inhibition is lethal to prokaryotes
-
malfunction
-
depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
-
malfunction
-
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
-
malfunction
-
because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
-
metabolism
biosynthesis of D-alanine as building blocks in the peptidoglycan layers of bacterial cell walls
metabolism
-
important for cell wall biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
important for peptidoglycan biosynthesis
metabolism
-
plays a role in spore germination and cell wall biosynthesis
metabolism
DadB expression is induced by L-alanine to a level much greater than that of Alr and is probably responsible for the catabolism of D-Ala. Alr is constitutively expressed and seems to provide the D-alanine necessary to maintain cell growth
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13) which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13) which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
important for peptidoglycan biosynthesis
-
metabolism
-
DadB expression is induced by L-alanine to a level much greater than that of Alr and is probably responsible for the catabolism of D-Ala. Alr is constitutively expressed and seems to provide the D-alanine necessary to maintain cell growth
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
physiological function
-
alanine racemase plays an essential role in cell wall synthesis as it racemizes L-alanine into D-alanine, a key building block in the biosynthesis of peptidoglycan
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
physiological function
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
physiological function
-
the pyridoxal 5'-phosphate-dependent enzyme alanine racemase produces the D-alanine incorporated in the cyclic peptide cyclosporine A synthesized by the fungus
physiological function
alanine racemase (Alr) is a bacterial enzyme that catalyses the conversion of L-Ala to D-Ala. This function is critical for the growth of bacteria due to their need for D-alanine, an essential component in the biosynthesis of cell wall peptidoglycan in both gram-positive and gram-negative bacteria2. Two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala. Enzyme Alr is essential for the growth and interspecies competitiveness of Streptococcus mutans, the major causative organism of dental caries
physiological function
alanine racemase (Alr) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible racemization of L- and D-alanine. D-alanine is an essential component of the bacterial cell-wall peptidoglycan
physiological function
Alkalihalophilus pseudofirmus
alanine racemase (Alr) is a pyridoxal 5'-phosphate-dependent (PLP) enzyme that catalyzes a reversible racemization between the enantiomers of alanine. D-Alanine is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan
physiological function
alanine racemase (ALR) is responsible for the high D-alanine production in Lactobacillus salivarius
physiological function
-
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
-
in addition to its function in the utilisation of D-alanine, Alr exhibits a role in protecting the system from inhibition by D-alanine
physiological function
in bacteria, two types of alanine racemase are encoded independently by two genes named dadX and alr. The dadX gene encodes a catabolic alanine racemase DadX, which catalyzes direct conversion of L-Ala to D-Ala. Its expression is induced by L- or D-Ala. The alr gene encodes an anabolic alanine racemase Alr, it is expressed constitutively at low level and essential for providing abundant D-Ala for peptidoglycan biosynthesis. The catabolic alanine racemase DadX usually shows much higher catalytic efficiency than the anabolic enzyme Alr. Essential role of Alr in D-Ala production
physiological function
-
in the absence of genes coding for alanine racemase Alr and DadX homologues in Chlamydia pneumonia a serine hydroxymethyl transferase GlyA serves as a source of D-Ala. D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and Alr2 can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
physiological function
the conversion of L-alanine (L-Ala) into D-alanine (D-Ala) in bacteria is performed by pyridoxal 5'-phosphate-dependent enzymes, alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival
physiological function
the enzyme catalyzes the interconversion of L-alanine to D-alanine. D-Alanine is an essential building block of the cell wall of both gram-positive and gram-negative bacteria
physiological function
the enzyme is an essential factor to maintain the growth and cell wall integrity of Streptococcus mutans
physiological function
the enzyme is responsible for racemization between enantiomers of alanine, D-alanine is an essential component of the bacterial cell wall
physiological function
-
the enzyme is an essential factor to maintain the growth and cell wall integrity of Streptococcus mutans
-
physiological function
-
alanine racemase (Alr) is a bacterial enzyme that catalyses the conversion of L-Ala to D-Ala. This function is critical for the growth of bacteria due to their need for D-alanine, an essential component in the biosynthesis of cell wall peptidoglycan in both gram-positive and gram-negative bacteria2. Two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala. Enzyme Alr is essential for the growth and interspecies competitiveness of Streptococcus mutans, the major causative organism of dental caries
-
physiological function
-
alanine racemase (ALR) is responsible for the high D-alanine production in Lactobacillus salivarius
-
physiological function
Alkalihalophilus pseudofirmus OF4
-
alanine racemase (Alr) is a pyridoxal 5'-phosphate-dependent (PLP) enzyme that catalyzes a reversible racemization between the enantiomers of alanine. D-Alanine is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan
-
physiological function
-
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and Alr2 can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
-
physiological function
-
alanine racemase (Alr) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible racemization of L- and D-alanine. D-alanine is an essential component of the bacterial cell-wall peptidoglycan
-
physiological function
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
the enzyme catalyzes the interconversion of L-alanine to D-alanine. D-Alanine is an essential building block of the cell wall of both gram-positive and gram-negative bacteria
-
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
-
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
-
physiological function
-
the conversion of L-alanine (L-Ala) into D-alanine (D-Ala) in bacteria is performed by pyridoxal 5'-phosphate-dependent enzymes, alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival
-
physiological function
-
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
-
physiological function
-
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
-
additional information
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
additional information
-
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
additional information
-
amino acid residues 319 and 364 are located directly in the active site. Y364 is involved in the positioning of the phosphate moiety of PLP and thus represents a prominent active site residue in the conserved inner layer of the substrate entrance corridor of Alr
additional information
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
additional information
-
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
additional information
Alkalihalophilus pseudofirmus
enzyme molecular structure analysis. The conserved residues at the substrate entryway and the salt bridge at the dimer interface are critical for enzyme activity
additional information
enzyme structure comparisons, active site structure, overview
additional information
-
enzyme structure comparisons, active site structure, overview
additional information
enzyme structure homology modeling using the crystal structure of Escherichia coli AlaR with PDB ID 2rjh
additional information
Residue Gln360 plays an essential role in substrate selection and has a preference for hydrophobic amino acids, especially Tyr, in bacterial alanine racemization. Enzyme structure determination and analysis, active site structure, detailed overview
additional information
structure-function realtionship analysis, overview
additional information
-
structure-function realtionship analysis, overview
additional information
comparisons of structure and function of CBL and ALR, overview
additional information
-
comparisons of structure and function of CBL and ALR, overview
additional information
Alkalihalophilus pseudofirmus OF4
-
enzyme molecular structure analysis. The conserved residues at the substrate entryway and the salt bridge at the dimer interface are critical for enzyme activity
-
additional information
-
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
-
additional information
-
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
-
additional information
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
enzyme structure homology modeling using the crystal structure of Escherichia coli AlaR with PDB ID 2rjh
-
additional information
-
structure-function realtionship analysis, overview
-
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120000 - 150000
-
gel filtration
33000
-
2 * 33000, SDS-PAGE
38000
-
2 * 38000, SDS-PAGE
38337
-
2 * 38337, calculated from amino acid sequence
38765
-
2 * 38765, calculated from amino acid sequence
38883
-
2 * 38883, calculated from amino acid sequence
38978
-
2 * 38978, calculated from amino acid sequence
39044
-
1 * 39044, calculation from nucleotide sequence
39068
-
2 * 39068, calculated from amino acid sequence
39075
-
2 * 39075, calculated from amino acid sequence
39152
-
2 * 39152, calculated from amino acid sequence
39700
-
1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
39800
-
1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
42500
2 * 42500, SDS-PAGE
42700
x * 42700, calculation from nucleotide sequence
42800
2 * 42800, recombinant enzyme, SDS-PAGE
43341
-
x * 43341, calculation from nucleotide sequence
43650
precided weight from primary sequence of 394 amino acids, yncD
43700
Q81VF6
2 * 43700, dynamic light scattering (DLS)
43810
Q81VF6
mass-spectrometry
44217
-
1 * 44217, calculated from amino acid sequence
44220
-
calculated from amino acid sequence
45770
-
x * 45770, calculated
46605
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
46621
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
46647
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
47000
x * 47000, recombinant His6-tagged enzyme, SDS-PAGE
48000
Alkalihalophilus pseudofirmus
mutant E134K, gel filtration
49000
Alkalihalophilus pseudofirmus
mutant D318K, gel filtration
58000
-
1 * 58000, SDS-PAGE
68000
gel-filtration analysis
69000
Alkalihalophilus pseudofirmus
mutant D70K, gel filtration
78630
Alkalihalophilus pseudofirmus
recombinant wild-type enzyme, gel filtration
80530
mutant enzyme, gel filtration
80640
Alkalihalophilus pseudofirmus
sequence calculation, wild-type enzyme
81090
wild-type enzyme, gel filtration
83000
gel filtration, recombinant enzyme
85000
-
HPLC gel filtration
86400
mutant enzyme, about, sequence calculation
86600
wild-type enzyme, about, sequence calculation
87000
Alkalihalophilus pseudofirmus
gel filtration
93000
Q81VF6
dynamic light scattering (DLS)
37000
-
3 or 4 * 37000, SDS-PAGE
37000
2 * 37000, SDS-PAGE
39000
-
1 * 39000, SDS-PAGE
39000
-
2 * 39000, SDS-PAGE
39000
-
2 * 39000, SDS-PAGE
39000
-
1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
39000
-
1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
39000
-
2 * 39000, SDS-PAGE, enzyme shows monomer-dimer equilibrium
39900
-
2 * 39900, calculated, 2 * 42000, SDs-PAGE
39900
2 * 39900, calculated, 2 * 42000, SDs-PAGE
40000
-
gel filtration
40000
Alkalihalophilus pseudofirmus
SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
40000
-
2 * 40000, SDS-PAGE
41000
Alkalihalophilus pseudofirmus
SDS-PAGE
42000
-
x * 42000, SDS-PAGE
42000
-
1 * 42000, SDS-PAGE
42000
-
2 * 39900, calculated, 2 * 42000, SDs-PAGE
42000
2 * 39900, calculated, 2 * 42000, SDs-PAGE
42000
-
x * 42000, recombinant His7-tagged enzyme, SDS-PAGE
43000
-
gel filtration
43000
-
1 * 43000, SDS-PAGE
43000
1 * 43000, SDS-PAGE
43000
1 * 43000, SDS-PAGE
43000
1 * 43000, SDS-PAGE
43000
1 * 43000, SDS-PAGE
43660
Q81VF6
immunoblotting
43660
-
x * 43660, sequence calculation
44000
gel filtration
44000
-
2 * 44000, SDS-PAGE
45000
-
SDS-PAGE
45000
-
enzyme including linker and His6-tag
45000
Alkalihalophilus pseudofirmus
mutant E71K, gel filtration
46000
gel filtration
46000
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
73000
gel filtration
73000
recombinant enzyme, dynamic light scattering
76000
-
gel filtration in presence or absence of 2-mercaptoethanol
76000
recombinant His-tagged wild-type enzyme, gel filtration
76000
Alkalihalophilus pseudofirmus
mutant D43K, gel filtration
78000
-
gel filtration
78000
-
equilibrium sedimentation method
80000
-
gel filtration
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tetramer
the Escherichia coli CBL tetramer (PDB entry 1CL1) adopts fold type I
?
-
x * 42000, recombinant His7-tagged enzyme, SDS-PAGE
?
-
x * 42000, recombinant His7-tagged enzyme, SDS-PAGE
-
?
x * 40390, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 40390, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43660, sequence calculation
?
-
x * 43660, sequence calculation
-
?
x * 42700, calculation from nucleotide sequence
?
x * 47000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 43341, calculation from nucleotide sequence
?
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 45770, calculated
?
-
3 or 4 * 37000, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE
-
dimer
enzyme structure comparisons, overview
dimer
Alkalihalophilus pseudofirmus
2 * 41000, gel filtration and dynamic light scattering
dimer
Alkalihalophilus pseudofirmus OF4
-
2 * 41000, gel filtration and dynamic light scattering
-
dimer
Q81VF6
crystallography
dimer
Q81VF6
2 * 43700, dynamic light scattering (DLS)
dimer
2 * 46000, recombinant His-tagged wild-type enzyme, SDS-PAGE, 2 * 46621, recombinant His-tagged wild-type enzyme, sequence calculation, 2 * 46605, recombinant His-tagged mutant S171A, sequence calculation, 2 * 46647, recombinant double-His-tagged mutant H359Y, sequence calculation
dimer
-
2 * 39000, SDS-PAGE
dimer
-
2 * 39900, calculated, 2 * 42000, SDs-PAGE
dimer
4 EcAlr monomers form 2 identical dimers, crystallography
dimer
the Escherichia coli ALR dimer (PDB entry 2RJG) adopts a fold type III
dimer
-
2 * 39000, SDS-PAGE
dimer
2 * 37000, SDS-PAGE
dimer
formed by two crystallographically different monomers, crystallization data
dimer
-
formed by two crystallographically different monomers, crystallization data
-
dimer
the enzyme exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites, a symmetric head-to-tail homodimer
dimer
-
the enzyme exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites, a symmetric head-to-tail homodimer
-
dimer
-
2 * 44000, SDS-PAGE
dimer
2 * 42500, SDS-PAGE
dimer
each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the pyridoxal 5'-phosphate cofactor and a second domain primarily composed of beta-strands
dimer
-
2 * 38000, SDS-PAGE
dimer
-
2 * 39000, SDS-PAGE, enzyme shows monomer-dimer equilibrium
dimer
-
2 * 39000, SDS-PAGE, enzyme shows monomer-dimer equilibrium
-
dimer
2 * 42800, recombinant enzyme, SDS-PAGE
dimer
-
2 * 42800, recombinant enzyme, SDS-PAGE
-
dimer
2 * 39900, calculated, 2 * 42000, SDs-PAGE
homodimer
-
homodimer
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
-
-
homodimer
Alkalihalophilus pseudofirmus
enzyme molecular structure analysis, the tertiary structure of DadXOF4 is a homodimer comprised of two monomers that interact in a head-to-tail manner. Each monomer is composed of two domains, an eight-stranded alpha/beta-barrel at the N-terminus and a C-terminal domain essentially composed of beta-strands. The dimer interface of DadXOF4 is formed by five pairs of salt bridges, i.e. Asp43-Lys360', Asp70-Lys2', Glu71-Arg361', Glu134-Arg259', and Asp318-Lys41'
homodimer
Alkalihalophilus pseudofirmus OF4
-
enzyme molecular structure analysis, the tertiary structure of DadXOF4 is a homodimer comprised of two monomers that interact in a head-to-tail manner. Each monomer is composed of two domains, an eight-stranded alpha/beta-barrel at the N-terminus and a C-terminal domain essentially composed of beta-strands. The dimer interface of DadXOF4 is formed by five pairs of salt bridges, i.e. Asp43-Lys360', Asp70-Lys2', Glu71-Arg361', Glu134-Arg259', and Asp318-Lys41'
-
homodimer
each monomer covers full-length AlrTt (Val1-Lys383), it contains an N-terminal eight-stranded alpha/beta barrel domain (residues 1-244) and a C-terminal extended beta-strand domain (residues 245-383). The active site is located in the center of alpha/beta barrel domain, it is surrounded by parallel beta strands. Two identical monomers associate at the C-terminal beta-strand domain and the alpha/beta barrel domain to form the functional dimer, enzyme structure determination and analysis, active site structure, detailed overview. A hydrophobic patch localizes underneath Gln360 and phosphate group of pyridoxal 5'-phosphate. This hydrophobic patch is conserved both in sequence and conformation among bacterial alanine racemase
homodimer
2 x 43306, recombinant wild-type enzyme, mass spectrometry, 2 * 43279, recombinant mutant enzyme, mass spectrometry
homodimer
-
2 x 43306, recombinant wild-type enzyme, mass spectrometry, 2 * 43279, recombinant mutant enzyme, mass spectrometry
-
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 39152, calculated from amino acid sequence
homodimer
computational simulations
homodimer
-
the homodimeric enzyme of 388 residues formed by a head-to-tail association of two monomers. Each monomer is composed of two folded domains: (i) an N-terminal domain formed by the portion 1-240 and (ii) a C-terminal domain with the remaining portion of the monomer (241-388). The N-terminal domain consists of an eight-stranded alpha/beta-barrel, while the C-terminal domain is made up of beta-strands. Molecular dynamics study
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 38337, calculated from amino acid sequence
homodimer
-
2 * 39068, calculated from amino acid sequence
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 38883, calculated from amino acid sequence
homodimer
-
2 * 38978, calculated from amino acid sequence
homodimer
-
2 * 40000, SDS-PAGE
-
homodimer
-
2 * 38883, calculated from amino acid sequence
-
homodimer
-
2 * 38978, calculated from amino acid sequence
-
homodimer
-
2 * 40000, SDS-PAGE
-
homodimer
-
2 * 38883, calculated from amino acid sequence
-
homodimer
-
2 * 38978, calculated from amino acid sequence
-
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 38765, calculated from amino acid sequence
homodimer
-
2 * 40000, SDS-PAGE
-
homodimer
-
2 * 38765, calculated from amino acid sequence
-
homodimer
-
2 * 40000, SDS-PAGE
homodimer
-
2 * 39075, calculated from amino acid sequence
homodimer
x-ray crystallography
homodimer
2 * 43400, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 43400, recombinant enzyme, SDS-PAGE
-
monomer
-
gel filtration
monomer
-
1 * 40500, SDS-PAGE
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
monomer
-
1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
monomer
-
1 * 39000, SDS-PAGE, 1 * 39700, calculated, enzyme shows monomer-dimer equilibrium
-
monomer
-
1 * 39000, SDS-PAGE, 1 * 39800, calculated, enzyme shows monomer-dimer equilibrium
-
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 44217, calculated from amino acid sequence
monomer
-
1 * 43000, SDS-PAGE
-
monomer
-
1 * 44217, calculated from amino acid sequence
-
monomer
-
1 * 39044, calculation from nucleotide sequence
monomer
-
1 * 39000, SDS-PAGE
monomer
-
dadB enzyme and alr enzyme
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
-
monomer
1 * 44000, SDS-PAGE
monomer
1 * 43000, SDS-PAGE
monomer
1 * 43000, SDS-PAGE
monomer
1 * 43000, SDS-PAGE
monomer
1 * 43000, SDS-PAGE
additional information
three-dimensional enzyme structure of the recombinnat His6-tagged enzyme, overview
additional information
the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
additional information
-
the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
additional information
-
the enzyme forms a homodimer with two active sites in which the cofactor pyridoxal 5'-phosphate is bound. Intermolecular interactions, overview
-
additional information
enzyme sequence and structure comparisons, overview
additional information
-
enzyme sequence and structure comparisons, overview
additional information
-
enzyme sequence and structure comparisons, overview
-
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
-
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
-
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
-
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
-
the monomeric enzyme interacts with other monomers in the presence of substrate
additional information
dimer interfaces for the enzyme is 2510 A2
additional information
-
dimer interfaces for the enzyme is 2510 A2
additional information
-
dimer interfaces for the enzyme is 2510 A2
-
additional information
enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
additional information
-
enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
additional information
-
enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
-
additional information
-
three-dimensional structure modeling of Tolypocladium inflatum alanine racemase based on the threonine aldolase crystal structure, homology modeling, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 9 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 15 mM NaCl, 10% v/v glycerol, 3 mM 2-mercaptoethanol, and 0.1 mM pyridoxal-5'-phosphate, with 0.001 ml of reservoir solution containing 2% v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate, pH 5.5, 16% w/v PEG 3350, equilibration against 1 ml of reservoir solution, method optimization, 2 days, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
purified recombinant enzyme, sitting drop vapour diffusion, 6 mg/ml protein solution is mixed with crystallization solution containing 100 mM MES, pH 6.0, 200 mM CaCl2, and 20% PEG 6000, 4 days, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement using the ligand- and water-free monomer structure of Pseudomonas aeruginosa as the search model
purified enzyme, hanging drop vapour diffusion, method, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement method using the crystal structure of native alanine racemase from Bacillus stearothermophilus as search model, PDB ID 1SFT
Alkalihalophilus pseudofirmus
using the hanging-drop vapour diffusion method at 291 K
Alkalihalophilus pseudofirmus
enzyme is subjected to a reductive-methylation procedure
Q81VF6
using the vapor diffusion method with sitting drops
Q81VF6
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 12 mg/ml protein in 10 mM Tris-HCl, pH 8.0 with 10 mM pyridoxal 5'-phosphate, with 0.1 M bis-tris pH 7.0, 22% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant His-tagged wild-type enzyme in complex with L-alanine and pyridoxal 5'-phosphate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl, pH 8.0, L-Ala and PLP at 1:1.5:1.5 molar ratio, with 0.001 ml of reservoir solution containing 22% PEG 4000, and 0.1 M Bis-Tris, pH 7.0, and equilibration against 0.3 ml reservoir solution, 16°C, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement using the alanine racemase from Bacillus stearothermophilus, PDB ID 1SFT, as a search model
wild-type enzyme in complex with pyridoxal-5'-phosphate or with D-cycloserine, and enzyme mutant K271T in complex with pyridoxal 5'-phosphate, sitting drop vapor diffusion method, mixing of 0.002 ml of 32 m/ml protein in 10 mM PLP, 1 mM TCEP, and 50 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% w/v PEG 3350 for the wild-type/PLP complex, and additional 100 mM cycloserine, 200 mM sodium formate, 20% w/v PEG 3350 for the wild-type enzyme/inhibitor complex, or containing 0.17 M lithium sulfate, 0.085 M Tris-HCl, pH 8.5, 25.5% w/v PEG 4000, and 20% v/v glycerol for the enzyme mutant/PLP complex, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution
hanging-drop vapor-diffusion method, protein concentration: 20 mg/ml; crystal screen buffer: 0.1 M HEPES, pH 8.0, 22% (w/v) PEG 8000, 0.3 M Ca-acetate, and 1/10 (v/v) cyclohexyl-methyl-beta-D-maltoside, drop: ratio 1/2 mixed protein solution and buffer (sum 2 microl) hanging over 1 ml of buffer; cryo-protecting solution: 0.1 M HEPES, pH 8.0, 22% (w/v) PEG 8000, 0.3 M Ca-acetate, 30% (v/v) glycerol and 1/10 (v/v) cyclohexyl-methyl-beta-D-maltoside for flashcooling in liquid nitrogen, diffracted to 2.5 A
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enzyme in complex with pyridoxyl 5'-phosphate and inhibitor acetate, PDB ID 1SFT
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hanging drop method using purified enzyme concentrated to 22 mg/ml. The hanging drop contains 0.01 ml of the protein solution, 0.01 ml of 23% polyethylene glycol 4K, 200 mM sodium acetate and 100 mM Tris, pH 8.5. Drops are equilibrated against 0.7 ml of polyethylene glycol 4K solution
hanging drop method, determination of the crystal structure of the (R)-1-aminoethylphosphonic acid-pyridoxal 5'-phosphate aldimine in complex with alanine racemase at 1.6 A resolution
hanging drop method, the structure of the enzyme with the inhibitor propionate bound in the active site is determined by X-ray crystallography to a resolution of 1.9 A
hanging-drop vapor diffusion method. Crystal structure of the enzyme bound with reaction intermediate analogs, N-(5'-phosphopyridoxyl)-L-alanine and N-(5'-phosphopyridoxyl)-D-alanine, determined at 2.0 A resolution with the crystallographic R factor of 17.2 for PLP-L-Ala and 16.9 for PLP-D-Ala complexes
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mutant Y265F in complex with D- and with L-cycloserine
study of water molecules by cluster analysis of several crystal structures
purified recombinant C-terminally His6-tagged selenomethionine-derivatized enzyme by sitting drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution with 0.002 ml of reservoir solution containing 25% PEG 3350, 0.1 M Bis-Tris, pH 5.5, 0.2 M sodium chloride, and equilibration against 0.650 ml of reservoir solution, X-ray diffraction structure determination and analysis at 1.7 A resolution via single wavelength anomalous dispersion
sitting drops equilibrated versus 1.5 M (NH4)2SO4, 2% polyethylene glycol 400 and 0.1 M HEPES, pH 7.5, crystal strcuture at 1.45 A resolution
purified recombinant enzyme from strain Mu50, sitting drop method, mixing of 12 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with 100 mM sodium acetate trihydrate, pH 5.0, and 1.8 M ammonium sulfate, 7 days, X-ray diffraction structure determination and analysis at 2.15 A resolution, molecular replacement
sitting drop vapor diffusion method
sitting drop vapor diffusion method, at 4°C in 1.2 M sodium citrate, 0.1 M MES, pH 7.2, and 10% (v/v) glycerol
purified recombinant N-terminally His-tagged enzyme free, or in complex with inhibitors D-cycloserine and propionate, sitting drop vapor diffusion, mixing of 0.001 ml of 20 mg/ml protein solution with 0.001 ml of crystallization solution containing 0.1 M Bis-Tris propane, pH 8.5, 0.2 M NaBr, 20% w/v PEG 3350, 38 days, X-ray diffraction structure determination and analysis at 2.8 A for the free enzyme, and at 1.51-1.64 A resolution for the enzyme complexes, model building
free enzyme and in complex with D- or L-cycloserine
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D318K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
D43K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
D70K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
E134K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
E71K
Alkalihalophilus pseudofirmus
site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
D318K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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D43K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
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D70K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, the mutant shows an altered structure and reduced activity compared to the wild-type enzyme
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E134K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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E71K
Alkalihalophilus pseudofirmus OF4
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site-directed mutagenesis, almost inactive mutant, the mutant shows an altered structure compared to the wild-type enzyme
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D48A
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no effect on the enzyme activity
deltaalr
Q81VF6
mutant with knocked out alanine racemase gene alr (2 alanine racemase-genes have been found in Bacillus anthracis jet)
K41A
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completely inactive
Y270A
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impaired enzyme activity
H359Y
site-directed mutagenesis
Q360A
site-directed mutagenesis, the mutant shows about 1.2fold increased activity compared to the wild-type enzyme
Q360C
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q360D
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Q360E
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
Q360F
site-directed mutagenesis, the mutant shows about 1.5fold increased activity compared to the wild-type enzyme
Q360G
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360H
site-directed mutagenesis, the mutant shows about 2.4fold increased activity compared to the wild-type enzyme
Q360I
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
Q360K
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Q360L
site-directed mutagenesis, the mutant shows about 2.5fold increased activity compared to the wild-type enzyme
Q360M
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360N
site-directed mutagenesis, the mutant shows about 2.3fold increased activity compared to the wild-type enzyme
Q360P
site-directed mutagenesis, the mutant shows about 1.5fold increased activity compared to the wild-type enzyme
Q360R
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360S
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Q360T
site-directed mutagenesis, the mutant shows about 1.8fold increased activity compared to the wild-type enzyme
Q360V
site-directed mutagenesis, the mutant shows about 2.3fold increased activity compared to the wild-type enzyme
Q360W
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
Q360Y
site-directed mutagenesis, the mutant shows 3fold increased activity compared to the wild-type enzyme
S171A
site-directed mutagenesis
S171A/H359Y
site-directed mutagenesis
S173D
site-directed mutagenesis
D164A
alanine racemase Alr from Escherichia coli with single point mutation from D to A at position 164
D164K
alanine racemase Alr from Escherichia coli with single point mutation from D to K at position 164
E165A
alanine racemase Alr from Escherichia coli with single point mutation from E to A at position 165
E165K
alanine racemase Alr from Escherichia coli with single point mutation from E to K at position 165
E221A
alanine racemase Alr from Escherichia coli with single point mutation from E to A at position 221
E221K
alanine racemase Alr from Escherichia coli with single point mutation from E to K at position 221
E221P
alanine racemase Alr from Escherichia coli with single point mutation from E to P at position 221
P219A
alanine racemase Alr from Escherichia coli with single point mutation from P to A at position 219
I222T
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
I222T/Y354W
site-directed mutagenesis, the double mutant is an alanine racemase with lysine racemization activity
R219E
catalytical active mutant, the catalytic effect in the Arg219Glu mutant enzyme is due to a combined solvent and inherent stabilizing effect of the protonated cofactor, in contrast to the wild-type enzyme where the catalytic effect may be ascribed to solvent effects alone
Y265A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
Y265F
1600fold reduction of racemization
Y354W
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
M319T
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the M319T mutation is positioned close enough to allow interaction with the D-cycloserine moiety, which, given the large change of the character of the side chain, can strongly affect D-cycloserine reactivity. M319 is located near Y364 and, as a result, it is possible that the M319T mutation alters the interaction with Y364, thereby affecting D-cycloserine inhibition. The M319T mutant enzyme shows minimal inhibition by D-cycloserine, even at 1 mM, the IC50 of this mutant cannot be determined
R373L
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the mutation is not directly located within the active site but near the dimer interface and close to residues M319 and D320, which play an important role in the makeup of the active site. The replacement of arginine with the short and hydrophobic side chain of leucine might disrupt molecular interactions at the dimer interface as well as destabilize the DCS binding site. The R373L mutation is not located directly within the active site, but also showa a significant increase in resistance to D-cycloserine, with an 27fold increased IC50 compared to the wild-type enzyme
Y364D
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the mutation to aspartic acid introduces a shorter and negatively charged side chain, which potentially affects pyridoxal 5'-phosphate orientation in the active site. The IC50 of the Y364D mutant for D-cycloserine shows a 50fold increase compared to the wild-type
K39A
site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the cofactor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
K39A
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site-directed mutagenesis, kinetically inactive mutant, the mutation disrupts the binding of the cofactor that is essential for catalysis (pyridoxal 5'-phosphate), the mutant shows altered binding kinetics with L-alanine and D-alanine, weak binding to L- and D-serine
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K39A
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mutant enzyme is inactive as a catalyst for racemization as well as transamination
K39A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
A131K
site-directed mutagenesis, the mutant shows a 3fold increased activity compared to wild-type
A131K
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site-directed mutagenesis, the mutant shows a 3fold increased activity compared to wild-type
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additional information
enzyme residue Gln360 and conformational changes of active site residues disrupt the hydrogen bonding interactions necessary for proper pyridoxal 5'-phosphate immobilization, and decrease both the substrate affinity and turnover number of AlrTt. Introduction of hydrophobic amino acids at Gln360 increase the racemase activity of AlrTt
additional information
construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
additional information
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construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
additional information
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construction of a alr2 knockout mutant RS07 generated by retargeting the pJS107 TargeTron plasmid. Complementation by expression of plasmid pRS89 encoding gene alr2. The alr2 mutant spores more readily germinate in response to L-alanine as a co-germinant, D-alanine also functions as a co-germinant, no germination in presence of taurocholic acid
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additional information
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DNA shuffling of enzyme genes from Salmonella typhimurium and Escherichia coli selecting clones that exhibit higher catalytic activity toward alanine as well as serine. Specific activities of selected clones were increased up to three times more than of wild types. One mutant achieves posttranslationally a high protein level
additional information
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additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
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in-frame deletion mutation, loss of ability to grow on D-alanine
additional information
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double mutant for the alr encoded enzyme and the dad B encoded enzyme display a phenotype of requirement for exogenous D-Ala for growth
additional information
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double mutant for the alr encoded enzyme and the dad B encoded enzyme display a phenotype of requirement for exogenous D-Ala for growth
additional information
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DNA shuffling of enzyme genes from Salmonella typhimurium and Escherichia coli selecting clones that exhibit higher catalytic activity toward alanine as well as serine. Specific activities of selected clones were increased up to three times more than of wild types. One mutant achieves posttranslationally a high protein level
additional information
construction of an alr mutant strain. D-Ala starvation causes cell morphology alterations of the alr mutant
additional information
upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Phenotype, overview. Decreased cariogenicity of alr-mutant strain in rats
additional information
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construction of an alr mutant strain. D-Ala starvation causes cell morphology alterations of the alr mutant
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additional information
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upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Phenotype, overview. Decreased cariogenicity of alr-mutant strain in rats
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31-54% sequence homologies with Bacillus subtilis and Salmonella typhimurium dadB and alr enzymes
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amplified by PCR, cloned and overexpressed in Escherichia coli BL21, both as native and His-tagged products
amplified by PCR, cloned and overexpressed with pOPINB in Escherichia coli Rosetta pLysS cells, His-tagged product
Q81VF6
amplified from genomic DNA from Enterococcus faecalis via PCR, integrated into pET22b, transformation of Escherichia coli BL21 (DE3) for overexpression as His-tagged protein
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analyzation of alanine racemase-transcripts (RT-PCR) during growth and sporulation of wild-type shows low transcription level during early and higher during late sporulation states, analyzed expression level (immunoblotting) shows only alanine racemase during late sporulating states, growth rate of alr-gene knockout mutant and wild-type are identical, mutant only produces half as many spores as wild-type, mutant and wild-type show same resistance against heat, lysozyme and organic solvents, germination takes place in mutant at lower levels of L-alanine (a suggested germination activator) than in wild-type (D-alanine ist suggested to inhibit germination when unfavourable growth conditions), conversion of phase-bright spores to phase-dark germinating cells takes already place within mother cells of the alr mutant (phase dark to phase light), not in wild-type cells resulting in non-resistant mutant-germinants and resistant wild-type-spores respectively
Q81VF6
cloning of two independent alanine racemases in Escherichia coli: Alr and DadX
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enzyme expression in Escherichia coli strain BL21(DE3)/pETALR
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enzyme expression in Escherichia coli strain BL21(DE3)/pMB1978
Escherichia coli strain BL21 (DE3) was transformed with pET28aAlr (1 wild-type and 8 single point mutants)
expressed as recombinant monomeric protein in Escherichia coli
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expressed in Escherichia coli as an N-terminal polyhistidine fusion
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
expressed in Escherichia coli strain ALA1
expression in Escherichia coli
expression in Escherichia coli as a His-tagged protein
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expression in Escherichia coli C600
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expression in Escherichia coli JM109
expression in Escherichia coli SOLR with a plasmid yYOK3
expression in Escherichia coli. Heterologous expression renders Saccharomyces cerevisiae capable of utilization of D-Ala as a nitrogen source but also relieves the yeast from the toxicity of D-Ala
expression of C-terminally His6-tagged selenomethionine-derivatized enzyme in Escherichia coli strain BL21(DE3) in HY medium
expression of soluble His-tagged NusA fusion enzyme in Escherichia coli strain HMS174(lambdaDE3)
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from muscle and hepatopancreas
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gene alr from strain OXA-23, DNA and amino acid sequence determination and analysis, expression of recombinant N-terminally His7-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene alr, expression of the enzyme in Escherichia coli strain BL21
gene alr, quantitative RT-PCR expression analysis
gene alr, recombinant expression in Escherichia coli strain BL21(DE3)
gene alr, recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene alr, sequence comparisons, recombinant expression of codon-optimized wild-type and mutant enzymes in Escherichia coli strain Rosetta 2 (pLysS)DE3, recombinant expression of wild-type and mutant enzymes in Escherichia coli alr/dadX double-knockout mutant strain MB2159, the wild-type and K271T mutant CdAlr proteins are able to complement the D-alanine auxotrophy and restore its growth in D-alanine-free medium
gene alr, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlusTM(DE3)-RIPL
gene alr, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star (DE3)pLysS
gene alr-2, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene alr-2, sequence comparisons, the gene encodes a functional enzyme that can complement the alanine racemase deficiency of Escherichia coli strain MB2795, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene alr1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene alr2, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene alrMB4, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene dadX, recombinant expression of wild-type and mutant enzymes
Alkalihalophilus pseudofirmus
gene MBalr2, DNA and amino acid sequence determination and analysis, expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme TmCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form
gene metC, phylogenetic analysis, the recombinant His6-tagged enzyme wMelCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Recombinant production of His6-tagged enzyme in a soluble form
gene metC, phylogenetic analysis, the recombinant MBP-tagged enzyme PuCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially. The enzyme rescues the alanine racemase knockout, Escherichia coli strain MB2795 (DELTAalrDELTAdadX), as quickly as expressing Escherichia coli ALR itself. Attempts to optimize recombinant production of the Pelagibacter ubique enzyme (PuCBL) in a soluble form are unsuccessful
gene metC, phylogenetic analysis. The recombinant enzyme EcCBL is overexpressed in a metC-deficient DELTAmetC Escherichia coli mutant strain and can complement it partially
isolation and sequencing of cDNA clones, nucleotide sequence 1798 bp including 5- and 3-nonreading frame, poly-A-tail and open reading frame of 1263 bp, expression in E. coli - transformed with open reading frame sequence in pET32Xa/LIC, produced fusion protein with alanine racemase by Escherichia coli, predicted molecular weight of fusion protein of 62000 Da (SDS-PAGE, immunoblotting)
recombinant expression in D-Alanine auxotrophic Escherichia coli strain MB2159 and DN1686, a D-Ala auxotrophic mutant
recombinant expression in D-Alanine auxotrophic Escherichia coli strains MB2159 and DN1686, a D-Ala auxotrophic mutant
strain has one single enzyme gene, expression in Escherichia coli with His-tag
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subcloned in a D-alanine auxotrophic Escherichia coli strain MB2795 and in Escherichia coli BL21(DE3)
two genes: dadA and dadB
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amplified by PCR, cloned and overexpressed in Escherichia coli BL21, both as native and His-tagged products
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amplified by PCR, cloned and overexpressed in Escherichia coli BL21, both as native and His-tagged products
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strain ALA1
expressed in Escherichia coli strain ALA1
expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli JM109
expression in Escherichia coli JM109
expression in Escherichia coli JM109
expression in Escherichia coli JM109
gene alr, recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene alr, recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
subcloned in a D-alanine auxotrophic Escherichia coli strain MB2795 and in Escherichia coli BL21(DE3)
Q81VF6
subcloned in a D-alanine auxotrophic Escherichia coli strain MB2795 and in Escherichia coli BL21(DE3)
Alkalihalophilus pseudofirmus
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