Information on EC 1.2.1.16 - succinate-semialdehyde dehydrogenase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.2.1.16
-
RECOMMENDED NAME
GeneOntology No.
succinate-semialdehyde dehydrogenase [NAD(P)+]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation III
-
-
Alanine, aspartate and glutamate metabolism
-
-
Butanoate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Nicotinate and nicotinamide metabolism
-
-
Tyrosine metabolism
-
-
glutamate and glutamine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate-semialdehyde:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-88-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain BW25113
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
; M5a1 strain and mutant M5a18
-
-
Manually annotated by BRENDA team
constitutive
-
-
Manually annotated by BRENDA team
strain ST-201
-
-
Manually annotated by BRENDA team
strain ST-201
-
-
Manually annotated by BRENDA team
Sprague-Dawley strain
-
-
Manually annotated by BRENDA team
Wistar strain
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
GABA metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
show the reaction diagram
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
show the reaction diagram
low dehydrogenase activity
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
show the reaction diagram
-
-
-
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
3-hydroxy-benzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
show the reaction diagram
-
-
-
?
4-chloro-benzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
show the reaction diagram
-
mandelate pathway
-
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
show the reaction diagram
beta-hydroxysuccinic semialdehyde + NADP+ + H2O
beta-hydroxysuccinate + NADPH + H+
show the reaction diagram
-
-
-
?
cyclohexanal + NAD+ + H2O
? + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
cyclohexanal + NAD+ + H2O
cyclohexanecarboxylic acid + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
show the reaction diagram
decanal + NADP+ + H2O
decanoate + NADPH + H+
show the reaction diagram
low dehydrogenase activity
-
-
?
heptanal + NAD+ + H2O
heptanoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
malonic semialdehyde + NADP+ + H2O
malonate + NADPH + H+
show the reaction diagram
-
hydrolyzed at 8.7% the rate of succinate semialdehyde
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
pentanal + NAD+ + H2O
pentanoate + NADH + H+
show the reaction diagram
-
good substrate
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
show the reaction diagram
-
-
-
-
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
show the reaction diagram
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
show the reaction diagram
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
show the reaction diagram
Q8ZPI3
low dehydrogenase activity
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
show the reaction diagram
-
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
show the reaction diagram
Q0K2K1
-
-
-
?
acetaldehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
show the reaction diagram
-
mandelate pathway
-
-
ir
decanal + NAD+ + H2O
decanoate + NADH + H+
show the reaction diagram
decanal + NADP+ + H2O
decanoate + NADPH + H+
show the reaction diagram
Q8ZPI3
low dehydrogenase activity
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
show the reaction diagram
Q0K2K1
-
-
-
-
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
slight activation
Mg2+
-
100% activity at 10 mM Mg2+. With Mg2+ there is a 4fold decrease in the Km value for succinate semialdehyde and a 6fold decrease in the Km value for NADP+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-tolualdehyde
-
only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5-dipropylpentanoate
-
-
coenzyme A
1 mM, 15% inhibition
dipropylacetate
-
-
glyoxylate
Malonic semialdehyde
N-ethylmaleimide
-
-
NADPH
p-chloromercuribenzoate
-
-
p-Hydroxybenzaldehyde
-
-
potassium arsenite
potassium phosphate buffer
-
-
succinate semialdehyde
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
4-aminobutyrate
induction during growth with 4-aminobutyrate (GABA)
4-aminobutyric acid
-
induction
dithiothreitol
gamma-aminobutyrate
-
induces GabD dehydrogenase
sulfhydryl reagents
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
2-oxoglutarate semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
0.041
3-sulfopropanal
Km apparent value
0.0069 - 0.035
benzaldehyde
0.0092 - 17
NAD+
0.038 - 27
NADP+
0.002 - 2.6
succinate semialdehyde
0.03
Succinic semialdehyde
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.1
2-oxoglutarate semialdehyde
Escherichia coli
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
6.4 - 57
benzaldehyde
2.7 - 176
NAD+
1.3 - 46
NADP+
0.3 - 164
succinate semialdehyde
22.6
Succinic semialdehyde
Escherichia coli
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
134.1
2-oxoglutarate semialdehyde
Escherichia coli
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
16028
3.8 - 880
NAD+
7
0.077 - 3066
NADP+
10
18 - 14700
succinate semialdehyde
528
3454
Succinic semialdehyde
Escherichia coli
-
in 0.1 M HEPES/KOH (pH 6.5), at 70C
809
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0628
succinate semialdehyde
-
in the absence of Mg2+, at pH 7.5 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
-
wild type, value below, NH4+ used as N-source or uga2 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.0025
-
wild type, glutamate used as N-source
0.0033
-
uga3 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.0038
H16-strain, coenzyme NAD+
0.0097
SK4580-strain, coenzyme NAD+
0.0105
HF39-strain, coenzyme NAD+
0.0172
SHF3-strain, coenzyme NAD+
0.021
-
wild type, succinate used as C-source, gamma-aminobutyrate and NH3 used as N-source
0.0235
SK4580-strain, coenzyme NADP+
0.0253
H16-strain, coenzyme NADP+
0.028
-
bis(3-aminopropyl)-amine used as C-source and N-source
0.029
-
spermidine used as C-source and N-source
0.03
-
bis(3-aminopropyl)-amine and glucose, glucose and NH3 or ribose and NH3 used as C-source and N-source
0.0319
SK4575-strain, coenzyme NAD+
0.032
-
gamma-aminobutyric acid and glucose used as C-source and N-source
0.033
-
spermidine and glucose used as C-source and N-source
0.034
-
wild type, 4-hydroxyphenylacetate used as C-source and NH3 used as N-source
0.035
-
gamma-aminobutyric acid used as C-source and N-source
0.0355
SK4575-strain, coenzyme NADP+
0.036
-
CS101A strain, unable to utilize 4-aminobutyrate as N-source
0.038
-
putrescine used as C-source and N-source
0.0409
HF39-strain, coenzyme NADP+
0.045
-
gamma-hydroxybutyric acid and NH3 used as C-source and N-source
0.0457
SHF3-strain, coenzyme NADP+
0.06
-
4-hydroxyphenylacetic acid and glucose used as carbon source, NH3 used as N-source
0.07
-
succinate used as carbon source, NH3 used as N-source
0.073
-
nutrient broth used as carbon source, NADP-dependent form
0.078
-
glycerol used as carbon source, 4-aminobutyric acid used as N-source
0.08
-
4-hydroxyphenylacetic acid used as carbon source, NH3 used as N-source
0.085
-
4-aminobutyric acid used as carbon source, NH3 used as N-source
0.089
-
mutant, glucose used as C-source and NH3 used as N-source
0.091
-
4-hydroxyphenylacetic acid, glucose and cAMP used as carbon source, NH3 used as N-source
0.097
-
mutant, succinate used as C-source and NH3 used as N-source
0.105
-
wild type, succinate used as C-source and gamma-aminobutyrate used as N-source
0.125
-
uga1 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.13
-
4-hydroxyphenylacetic acid and cAMP used as carbon source, NH3 used as N-source
0.319
-
mutant, gamma-aminobutyrate used as C-source and NH3 used as N-source
0.351
-
mutant, succinate used as C-source and gamma-aminobutyrate used as N-source
0.38
-
wild type, glutamate and 4-aminobutyric acid used as N-source
0.395
-
mutant, glucose used as C-source and gamma-aminobutyrate used as N-source
0.408
-
mutant, gamma-aminobutyrate used as C-source and as N-source
0.5 - 0.66
-
wild type, 4-aminobutyric acid used as N-source
0.731
-
CS101G2 strain, unable to utilize 4-aminobutyrate as N-source
0.797
-
S-5 strain, unable to utilize 4-aminobutyrate as N-source
1.012
-
S-9 strain, unable to utilize 4-aminobutyrate as N-source
1.023
-
L-18 strain, unable to utilize 4-aminobutyrate as N-source
1.038
-
D-8 strain, unable to utilize 4-aminobutyrate as N-source
1.08
-
M-20 strain, unable to utilize 4-aminobutyrate as N-source
1.264
-
CS101B strain, able to utilize 4-aminobutyrate as N-source
40.7
-
pH 8.0, 30C
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
KM value for NAD+ increases from 0.3 to 1 mM as the pH changes from pH 5 to 10. The pH profile data are obtained at a NAD+ concentration of 5 mM, essentially saturating across the entire pH range. Similarly, data for the NADP+ pH profile are obtained at 10 mM NADP+
5.5 - 10
-
the enzyme cannot be assayed below pH 5.5, due to precipitation and loss of activity
7 - 9.3
-
at pH 7.0 and 9.3: about 30% of activity maximum
7.5 - 9.5
-
-
8 - 10.5
specific activity increases steadily to a broad optimum
8.7 - 10.6
-
with NAD+, at pH 8.7: 45% of activity maximum, at pH 10.6: about 50% of activity maximum
8.7 - 10.9
-
with NADP+, at pH 8.7: about 30% of activity maximum, at pH 10.9: about 65% of activity maximum
additional information
-
The pH profiles are bell-shaped indicating that two ionizable groups are involved in the catalytic mechanism.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
35 - 45
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella abortus (strain 2308)
Burkholderia pseudomallei (strain 1710b)
Escherichia coli (strain K12)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
2 * 45000, in solution, SDS-PAGE,
47400
-
calculated from amino acid sequence
51600
-
2 * 51600, SDS-PAGE
53000
-
2 * 53000, SDS-PAGE
59000
-
4 * 59000, SDS-PAGE
90000
-
Dimer is determined by gel filtration whereas the molecular mass of the enzyme is calculated by comparison to the relative mobility of the standard proteins.; SDS-PAGE
100000
-
gel filtration
114000
-
gel filtration
150000
-
gel filtration
180000
gel filtration
200000
-
gel filtration
275000
-
gel filtration
300000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-form and in complex with NAD+, hanging drop vapor diffusion method, using 2 M sodium formate and 0.1 M sodium acetate (pH 4.6), at 22C
apoenzyme and in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M MES monohydrate pH 5.8-6.1 and 18-23% (w/v) polyethylene glycol 4000
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
enzyme is almost inactive
698627
5 - 10
-
the Km value for NAD+ increases from 0.3 to 1 mM as the pH changes from pH 5 to 10
685387
6.5 - 7.1
-
highest stability
288041, 288046
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 2
-
substancial progressive loss of activity, sucrose fractions
25
-
substancial progressive loss of activity, sucrose fractions
60
-
up to, in presence of 30% glycerol
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol is necessary both to maintain the activity of BADH and to prevent oligimerization of the enzyme
-
enzyme is labile (50% loss of activity overnight) but can be largely stabilized (in crude extract only) by the addition of 10 mM dithiothreitol 1.2.1.16
ethyleneglycol, 30%, stabilizes
-
glycerol, 30%, stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
there is no significant loss of catalytic activity, after up to 40 min of incubation of isoform GabD1 with 1 mM H2O2 at pH 7.4
-
724115
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2C, pH 7.0, 10% loss of activity per week
-
3C or -15C, overnight, 100% loss of activity, without mercaptoethanol
-
5C, complete inactivation after 2 days
-
Addition of 2 mM DTT to both stacking and resolving gels results in a decrease in the protein laddering effect, and both BADH and BADH-His are present as near-homogeneous species.
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation and DEAE-cellulose
-
ammonium sulfate fractionation, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
-
by ammonium sulfate precipitation and anion exchange chromatography and gel filtration
chromatography on Celite 535
-
chromatography on Sephacryl S-300, DEAE-Sephacel and Sepharose 4B
-
column chromatography on DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex
-
DEAE-cellulose chromatography
-
His-tagged GabD dehydrogenase purified from cell extracts with HiTrap affinity columns
-
Ni-NTA resin column chromatography
-
Ni-NTA resin column chromatography and Superdex 75 gel filtration
Ni2+-agarose chromatography; Purification of his-tagged proteins by using a standard Ni2+-agarose chromatography protocol.
-
polyanionic resin Polyanion S1-HR5/5
-
UNO Q-12 column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
expressed in Escherichia coli strain BL21(DE3)pLysS; Protein expression in Escherichia coli strain JM109. Single colonies are picked and the DNA is isolated and screened for the desired mutation either by restriction analysis (C103A and C249A) or by sequencing (C140A and C220A). The overall fidelity of the PCR amplification and the presence of the desired mutations are confirmed by sequencing. The plasmids containing the mutated genes are then transformed into Escherichia coli strain BL21(DE3)pLysS for protein expression.
-
expression in Escherichia coli
gabD gene cloned, expression in Escherichia coli
overexpressed as His-tagged GabD
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by exogenous succinic semialdehyde
-
induction by growth on 4-hydroxyphenylacetate
-
transcript is detected inducibly in both homotaurine and GABA-grown cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C311A
-
mutant is still soluble but unable to catalyze succinate semialdehyde oxidation. Mutation leads to an inactive product binding both succinate semialdehyde aldehyde and gem-diol
C102A
-
mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
C103A
-
enzyme is inactive
C140A
-
activity between 50 and 75% in comparison to wild-type; mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
C220A
-
activity between 50 and 75% in comparison to wild-type; mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
C249A
-
activity between 50 and 75% in comparison to wild-type; inactive
D426A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E442A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F138A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160E
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K92A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N193A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R145A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R428A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S425A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W141A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D426A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
F138A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
K160A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
N193A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
S425A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
S434A
kinetic data show no significant difference from wild-type enzyme
S434D
kinetic data show no significant difference from wild-type enzyme
S434E
kinetic data show no significant difference from wild-type enzyme
S434A
-
kinetic data show no significant difference from wild-type enzyme
-
S434D
-
kinetic data show no significant difference from wild-type enzyme
-
S434E
-
kinetic data show no significant difference from wild-type enzyme
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Show AA Sequence (4335 entries)
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