BRENDA - Enzyme Database show
show all sequences of 4.3.3.6

On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis

Raschle, T.; Amrhein, N.; Fitzpatrick, T.B.; J. Biol. Chem. 280, 32291-32300 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
acivicin
inhibition of the glutaminase domain YuaaD, and thus pyridoxal 5'-phosphate synthesis
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.068
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.077
-
D-glyceraldehyde 3-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.99
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
1.0 mM Mn2+, Mg2+, Co2+, Ca2+, Ni2+, Fe3+, Fe2+, Cu3+, Cu2+, or Zn2+ has no effect on activity
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
Bacillus subtilis
the enzyme is involved in vitamin B6 biosynthesis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
the enzyme is involved in vitamin B6 biosynthesis
715478
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions
715478
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Both the glutaminase and synthase reactions are dependent on the respective protein partner. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions
715478
Bacillus subtilis
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
?
L-glutamine + H2O
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Glutaminase activity of YaaE is only detected in the presence of its partner protein YaaD. A 1:1 stoichiometry of both proteins appears to be optimal for activity
715478
Bacillus subtilis
L-glutamate + NH3
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00033
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.127
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acivicin
inhibition of the glutaminase domain YuaaD, and thus pyridoxal 5'-phosphate synthesis
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.068
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.077
-
D-glyceraldehyde 3-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.99
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
1.0 mM Mn2+, Mg2+, Co2+, Ca2+, Ni2+, Fe3+, Fe2+, Cu3+, Cu2+, or Zn2+ has no effect on activity
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
Bacillus subtilis
the enzyme is involved in vitamin B6 biosynthesis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
the enzyme is involved in vitamin B6 biosynthesis
715478
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions
715478
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Both the glutaminase and synthase reactions are dependent on the respective protein partner. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions
715478
Bacillus subtilis
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
?
L-glutamine + H2O
two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Glutaminase activity of YaaE is only detected in the presence of its partner protein YaaD. A 1:1 stoichiometry of both proteins appears to be optimal for activity
715478
Bacillus subtilis
L-glutamate + NH3
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Bacillus subtilis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00033
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.127
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Bacillus subtilis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.044
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.128
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.044
-
D-ribose 5-phosphate
pH 8.0, 37°C
Bacillus subtilis
0.128
-
L-glutamine
pH 8.0, 37°C
Bacillus subtilis
Other publictions for EC 4.3.3.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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1
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2
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-
1
-
-
-
-
-
3
1
-
-
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3
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
3
-
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1
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1
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-
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-
-
-
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-
-
-
1
-
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1
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1
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1
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-
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1
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5
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5
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-
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3
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1
-
-
-
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-
1
-
-
-
-
-
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-
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-
-
5
-
-
1
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-
5
-
5
5
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1
-
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-
1
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-
-
729134
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1
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1
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3
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1
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1
-
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-
-
-
-
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-
4
4
-
-
-
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2013
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2
-
1
-
-
-
-
-
-
3
-
5
-
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-
3
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3
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1
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3
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-
3
-
-
-
-
-
-
-
-
-
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2
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-
-
-
721233
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Overexpression, crystallizatio ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
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68
440-442
2012
-
-
1
1
-
-
-
-
-
-
2
-
-
9
-
-
1
-
-
-
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1
1
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2
-
2
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2
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1
-
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-
1
1
-
-
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-
-
-
-
-
-
-
-
-
-
-
723192
Matsuura
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Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Mol. Cells
34
407-412
2012
-
-
1
1
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
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-
1
-
1
-
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-
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1
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-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726499
Guedez
Assembly of the eukaryotic PLP ...
Plasmodium berghei, Plasmodium falciparum
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20
172-184
2012
-
-
2
2
8
-
-
-
-
-
-
-
-
4
-
-
2
-
-
-
28
-
4
2
-
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-
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-
-
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2
-
2
8
-
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2
-
-
28
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
716150
Jochmann
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Corynebacterium glutamicum, Corynebacterium glutamicum NJ0898
Microbiology
157
77-88
2011
-
-
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-
-
-
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2
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-
-
-
2
1
1
2
-
-
726269
Moccand
It takes two to Tango: Definin ...
Bacillus subtilis
PLoS ONE
6
e16042
2011
-
-
1
-
8
-
-
24
-
-
1
-
-
1
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1
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1
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13
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1
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8
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24
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1
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1
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1
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-
13
-
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25
25
724219
Zhang
Structural insights into the c ...
Saccharomyces cerevisiae
Biochem. J.
432
445-450
2010
-
-
1
1
6
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6
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1
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1
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1
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6
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1
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1
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724999
Derrer
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584
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-
-
1
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7
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2
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1
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1
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2
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2
1
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7
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1
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2
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2
1
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714170
Wallner
Dissection of contributions fr ...
Bacillus subtilis
Biochemistry
48
1928-1935
2009
-
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1
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10
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2
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1
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1
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1
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10
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1
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1
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713758
Hanes
Trapping of a chromophoric int ...
Bacillus subtilis
Angew. Chem. Int. Ed. Engl.
47
2102-2105
2008
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-
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1
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716306
Hanes
13C NMR snapshots of the compl ...
Bacillus subtilis
Nat. Chem. Biol.
4
425-430
2008
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1
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1
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2
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1
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2
-
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-
-
-
715491
Raschle
Reaction mechanism of pyridoxa ...
Bacillus subtilis
J. Biol. Chem.
282
6098-6105
2007
-
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5
-
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2
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3
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2
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1
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4
1
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5
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2
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2
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1
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4
1
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2
2
716736
Strohmeier
Structure of a bacterial pyrid ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
103
19284-19289
2006
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1
1
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5
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1
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1
1
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1
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1
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1
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1
1
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715247
Burns
Reconstitution and biochemical ...
Bacillus subtilis
J. Am. Chem. Soc.
127
3682-3683
2005
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715478
Raschle
On the two components of pyrid ...
Bacillus subtilis
J. Biol. Chem.
280
32291-32300
2005
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3
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