BRENDA - Enzyme Database
show all sequences of 2.6.99.3

. Establishment of an in vitro D-cycloserine-synthesizing system by using O-ureido-L-serine synthase and D-cycloserine synthetase found in the biosynthetic pathway

Uda, N.; Matoba, Y.; Kumagai, T.; Oda, K.; Noda, M.; Sugiyama, M; Antimicrob. Agents Chemother. 57, 2603-2612 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Streptomyces lavendulae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
9
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
4 * 36000, SDS-PAGE
Streptomyces lavendulae
126000
-
gel filtration
Streptomyces lavendulae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-acetyl-L-serine + hydroxyurea
Streptomyces lavendulae
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
O-ureido-L-serine + acetate
-
-
?
O-acetyl-L-serine + hydroxyurea
Streptomyces lavendulae ATCC 11924
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
O-ureido-L-serine + acetate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces lavendulae
D2Z027
-
-
Streptomyces lavendulae ATCC 11924
D2Z027
-
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces lavendulae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-acetyl-L-serine + hydroxyurea
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
721306
Streptomyces lavendulae
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O3-acetyl-D-serine and L-serine. The enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme also catalyzes the reaction with O-acetyl-L-serine and hydrogen sulfide (with 80fold higher catalytic efficiency)
721306
Streptomyces lavendulae
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
721306
Streptomyces lavendulae ATCC 11924
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O3-acetyl-D-serine and L-serine. The enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme also catalyzes the reaction with O-acetyl-L-serine and hydrogen sulfide (with 80fold higher catalytic efficiency)
721306
Streptomyces lavendulae ATCC 11924
O-ureido-L-serine + acetate
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 36000, SDS-PAGE
Streptomyces lavendulae
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Streptomyces lavendulae
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Streptomyces lavendulae
9
-
activity increases from pH 5.0 to pH 9.0
Streptomyces lavendulae
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.5
9
activity at pH 7.5 is about 45% compared to activity at pH 9.0
Streptomyces lavendulae
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Streptomyces lavendulae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
9
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
4 * 36000, SDS-PAGE
Streptomyces lavendulae
126000
-
gel filtration
Streptomyces lavendulae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-acetyl-L-serine + hydroxyurea
Streptomyces lavendulae
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
O-ureido-L-serine + acetate
-
-
?
O-acetyl-L-serine + hydroxyurea
Streptomyces lavendulae ATCC 11924
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
O-ureido-L-serine + acetate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Streptomyces lavendulae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-acetyl-L-serine + hydroxyurea
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
721306
Streptomyces lavendulae
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O3-acetyl-D-serine and L-serine. The enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme also catalyzes the reaction with O-acetyl-L-serine and hydrogen sulfide (with 80fold higher catalytic efficiency)
721306
Streptomyces lavendulae
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
721306
Streptomyces lavendulae ATCC 11924
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O3-acetyl-D-serine and L-serine. The enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme also catalyzes the reaction with O-acetyl-L-serine and hydrogen sulfide (with 80fold higher catalytic efficiency)
721306
Streptomyces lavendulae ATCC 11924
O-ureido-L-serine + acetate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 36000, SDS-PAGE
Streptomyces lavendulae
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Streptomyces lavendulae
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Streptomyces lavendulae
9
-
activity increases from pH 5.0 to pH 9.0
Streptomyces lavendulae
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.5
9
activity at pH 7.5 is about 45% compared to activity at pH 9.0
Streptomyces lavendulae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.15
-
O-acetyl-L-serine
30C, pH 8.0, cosubstrate: hydroxyurea
Streptomyces lavendulae
1.2
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.15
-
O-acetyl-L-serine
30C, pH 8.0, cosubstrate: hydroxyurea
Streptomyces lavendulae
1.2
-
Hydroxyurea
30C, pH 8.0
Streptomyces lavendulae
Other publictions for EC 2.6.99.3
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)
737505
Kumagai
High-level heterologous produc ...
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
Appl. Environ. Microbiol.
81
7881-7887
2015
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
738218
Uda
The structural and mutational ...
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
FEBS J.
282
3929-3944
2015
-
-
1
1
6
-
-
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
4
1
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
1
6
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
4
1
-
-
-
2
-
-
-
-
-
-
-
-
6
6
721306
Uda
. Establishment of an in vitro ...
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
Antimicrob. Agents Chemother.
57
2603-2612
2013
-
-
1
-
-
-
-
1
-
-
2
2
-
6
-
-
1
-
-
-
-
-
4
1
1
-
-
1
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
2
-
-
-
1
-
-
-
-
4
1
1
-
-
1
2
1
-
-
-
-
-
-
2
2
721300
Kumagai
Molecular cloning and heterolo ...
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
Antimicrob. Agents Chemother.
54
1132-1139
2010
-
-
-
-
-
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-