BRENDA - Enzyme Database
show all sequences of 6.3.2.49

ywf in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase

Tabata, K.; Ikeda, H.; Hashimoto, S.; J. Bacteriol. 187, 5195-5202 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Bacillus subtilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
CdSO4
2 mM, complete inhibition
Bacillus subtilis
ZnSO4
2 mM, complete inhibition
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
L-glutamine
pH 9.0, 37°C
Bacillus subtilis
0.42
-
ATP
pH 9.0, 37°C
Bacillus subtilis
105
-
L-alanine
pH 9.0, 37°C
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
Mg2+ or Mn2+ is essential for activity
Bacillus subtilis
Mn2+
Mg2+ or Mn2+ is essential for activity
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Bacillus subtilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
P39641
-
-
Bacillus subtilis 168
P39641
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-alanine + L-glutamine
GTP does not substitute for ATP
662037
Bacillus subtilis
ADP + phosphate + L-alanyl-L-glutamine
-
-
-
?
ATP + L-alanine + L-glutamine
GTP does not substitute for ATP
662037
Bacillus subtilis 168
ADP + phosphate + L-alanyl-L-glutamine
-
-
-
?
additional information
while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine
662037
Bacillus subtilis
?
-
-
-
-
additional information
while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine
662037
Bacillus subtilis 168
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Bacillus subtilis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus subtilis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
45
25°C: about 70% of maximal activity, 45°C: about 55% of maximal activity
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
-
Bacillus subtilis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8.5
10.5
pH 8.5: about 70% of maximal activity, pH 10.5: about 35% of maximal activity
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Bacillus subtilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
CdSO4
2 mM, complete inhibition
Bacillus subtilis
ZnSO4
2 mM, complete inhibition
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
L-glutamine
pH 9.0, 37°C
Bacillus subtilis
0.42
-
ATP
pH 9.0, 37°C
Bacillus subtilis
105
-
L-alanine
pH 9.0, 37°C
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
Mg2+ or Mn2+ is essential for activity
Bacillus subtilis
Mn2+
Mg2+ or Mn2+ is essential for activity
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
x * 53000, SDS-PAGE
Bacillus subtilis
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
ATP + L-alanine + L-glutamine
GTP does not substitute for ATP
662037
Bacillus subtilis
ADP + phosphate + L-alanyl-L-glutamine
-
-
-
?
ATP + L-alanine + L-glutamine
GTP does not substitute for ATP
662037
Bacillus subtilis 168
ADP + phosphate + L-alanyl-L-glutamine
-
-
-
?
additional information
while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine
662037
Bacillus subtilis
?
-
-
-
-
additional information
while the enzyme has extremely broad substrate specificity, some preferences are observed; the enzyme does not accept highly charged amino acids such as Lys, Arg, Glu, and Asp. The enzyme does not react with secondary amines such as Pro. The N-terminal residue of the dipeptide formed seems to be limited to Ala, Gly, Ser, Thr, and Met whereas the C-terminal residue seems to allow for a wider array of amino acids; and Ala and Ser seems to be most preferred for the N-terminal residue while Met and Phe seems to be preferred for the C-terminus. The enzyme does not react with D-Ala, D-serine, or D-phenylalanine
662037
Bacillus subtilis 168
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 53000, SDS-PAGE
Bacillus subtilis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus subtilis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
45
25°C: about 70% of maximal activity, 45°C: about 55% of maximal activity
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9.5
-
-
Bacillus subtilis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8.5
10.5
pH 8.5: about 70% of maximal activity, pH 10.5: about 35% of maximal activity
Bacillus subtilis
Other publictions for EC 6.3.2.49
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)
733347
Tsuda
Single mutation alters the sub ...
Bacillus subtilis
Biochemistry
53
2650-2660
2014
-
1
-
1
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726743
Arai
L-amino acid ligase from Pseud ...
Pseudomonas syringae, Pseudomonas syringae NBRC 14081
Appl. Environ. Microbiol.
79
5023-5029
2013
-
1
1
-
-
-
-
-
-
1
-
4
-
4
-
-
-
-
-
-
-
-
100
-
1
1
-
-
1
1
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
100
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
729244
Parker
Action and timing of BacC and ...
Bacillus subtilis 168, Bacillus subtilis
Biochemistry
52
889-901
2013
-
-
1
-
-
-
-
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726581
Suzuki
The structure of L-amino-acid ...
Bacillus licheniformis, Bacillus licheniformis NBRC 12200
Acta Crystallogr. Sect. D
68
1535-1540
2012
-
-
1
1
-
-
-
-
-
1
-
2
-
4
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
726615
Tsuda
Crystallization and preliminar ...
Bacillus subtilis 168, Bacillus subtilis
Acta Crystallogr. Sect. F
68
203-206
2012
-
-
-
1
1
-
-
-
-
-
2
-
-
7
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
730896
Shomura
Structural and enzymatic chara ...
Bacillus subtilis 168, Bacillus subtilis
Protein Sci.
21
707-716
2012
-
1
1
1
2
-
1
12
-
-
-
2
-
6
-
-
1
-
-
-
-
-
6
1
1
-
-
10
1
-
-
-
1
-
-
-
1
1
-
1
2
-
-
1
1
12
-
-
-
2
-
-
-
1
-
-
-
-
6
1
1
-
-
10
1
-
-
-
-
-
-
-
-
-
702768
Kino
A novel L-amino acid ligase fr ...
Bacillus subtilis, Bacillus subtilis NBRC3134
Biosci. Biotechnol. Biochem.
74
129-134
2010
-
-
1
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
1
1
-
-
-
1
1
-
-
-
702771
Senoo
Identification of novel L-amin ...
Actinobacillus pleuropneumoniae, Photorhabdus laumondii subsp. laumondii, Streptococcus mutans, Streptococcus pneumoniae, Treponema denticola
Biosci. Biotechnol. Biochem.
74
415-418
2010
-
-
5
-
-
-
-
-
-
-
-
-
-
5
-
-
5
-
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
115
-
5
-
-
-
5
-
-
-
-
-
-
-
-
-
690733
Kino
Dipeptide synthesis by L-amino ...
Ralstonia solanacearum, Ralstonia solanacearum JCM 10489
Biochem. Biophys. Res. Commun.
371
536-540
2008
-
-
1
-
-
-
-
1
-
1
1
2
-
4
-
-
1
-
-
-
-
-
4
1
1
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
1
2
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
693286
Kino
A novel L-amino acid ligase fr ...
Bacillus licheniformis, Bacillus licheniformis NBRC12200
J. Biosci. Bioeng.
106
313-315
2008
-
-
1
-
-
-
-
-
-
1
-
4
-
4
-
-
1
-
-
-
-
-
17
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
1
-
-
-
-
17
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
671498
Tabata
Fermentative production of L-a ...
Bacillus subtilis
Appl. Environ. Microbiol.
73
6378-6385
2007
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662037
Tabata
ywf in Bacillus subtilis codes ...
Bacillus subtilis, Bacillus subtilis 168
J. Bacteriol.
187
5195-5202
2005
-
-
1
-
-
-
2
3
-
2
1
-
-
7
-
-
1
-
-
-
-
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
3
-
2
1
-
-
-
-
1
-
-
-
-
4
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
733219
Steinborn
bac genes for recombinant baci ...
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens ATCC 15841, Bacillus pumilus, Bacillus pumilus ATCC 7065, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis A1/3, no activity in Bacillus amyloliquefaciens, no activity in Bacillus amyloliquefaciens GSB272, no activity in Bacillus coagulans, no activity in Bacillus licheniformis, no activity in Bacillus licheniformis ATCC 9789, no activity in Bacillus megaterium, no activity in Bacillus megaterium PV361, no activity in Bacillus pumilus, no activity in Bacillus pumilus ATCC 12140
Arch. Microbiol.
183
71-79
2005
-
-
3
-
1
-
-
-
-
3
-
8
-
21
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
3
-
-
-
-
-
4
4
-
1
-
-
-
-
-
-
4
-
8
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
6
7
-
-
-