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Information on EC 2.6.99.3 - O-ureido-L-serine synthase
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2.6.99.3 O-ureido-L-serine synthaseIUBMB Comments
The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species. Also catalyses EC 2.5.1.47, cysteine synthase.
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The enzyme appears in viruses and cellular organisms
Synonyms
DcsD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DcsD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydroxyurea = O-ureido-L-serine + acetate
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
O-acetyl-L-serine:hydroxyurea 2-amino-2-carboxyethyltransferase
The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species. Also catalyses EC 2.5.1.47, cysteine synthase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
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)
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-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
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)
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
-
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
O-ureido-L-serine i.e. (2S)-2-amino-3-[(carbamoylamino)oxy]propanoate
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
-
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of L-cysteine from O-acetyl-L-serine and H2S, reaction of EC 2.5.1.47. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
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-
?
additional information
?
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enzyme additionally catalyzes the formation of L-cysteine from O-acetyl-L-serine and H2S, reaction of EC 2.5.1.47. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
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-
?
additional information
?
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enzyme additionally catalyzes the formation of L-cysteine from O-acetyl-L-serine and H2S, reaction of EC 2.5.1.47
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-
?
additional information
?
-
enzyme additionally catalyzes the formation of L-cysteine from O-acetyl-L-serine and H2S, reaction of EC 2.5.1.47. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
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-
?
additional information
?
-
enzyme additionally catalyzes the formation of L-cysteine from O-acetyl-L-serine and H2S, reaction of EC 2.5.1.47
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
the enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
O-acetyl-L-serine
30°C, pH 8.0, cosubstrate: hydroxyurea
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9
activity at pH 7.5 is about 45% compared to activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2S6TY24_9PROT
360
0
38861
TrEMBL
-
A0A2S6TCA0_9PROT
363
0
39308
TrEMBL
-
A0A5B8RC10_9ZZZZ
361
0
39231
TrEMBL
other Location (Reliability: 2)
A0A6A7SFN3_9ZZZZ
361
0
39231
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
both in solution and in a crystalline state, crystallization data
tetramer
-
both in solution and in a crystalline state, crystallization data
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant K43A, to 2.25 and 1.9 A resolution, respectively. Each monomer of DcsD takes a typical fold of type II pyridoxal 5'-phosphate enzymes with the cofactor pyridoxal 5'-phosphate covalently bound to invariant Lys residue (Lys43) at the active site. The pyridine ring of pyridoxal 5'-phoshate makes hydrogen bonds with invariant Asn73 and Ser265 residues. Its phosphate group makes hydrogen bonds with Gly177, Thr178, Thr179 and Thr181 residues
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K43A
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
S121A
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
S121M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
V74T
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97F
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
expression of a D-cycloserine biosynthetic gene cluster consisting of 10 open reading frames (dcsA to dcsJ) from Streptomyces lavendulae ATCC 11924 in Escherichia coli. When L-serine and hydroxyurea, the precursors of D-cycloserine, are incubated together with the Escherichia coli resting cell suspension, the cells produce significant amounts of D-cycloserine (350 microM). To increase the productivity, the dcsJ gene, which might be responsible for the excretion, is connected downstream of the four genes, resulting in production of D-cycloserine at 660 microM. To repress the side catalytic activity of DcsD, i.e. the formation of L-cysteine from O-acetylserine and H2S, Escherichia coli chromosomal cysJ and cysK genes, encoding the sulfite reductase alpha subunit and O-acetylserine sulfhydrylase, respectively, are disrupted. The final strain produces 980 microM D-cycloserine
synthesis
-
expression of a D-cycloserine biosynthetic gene cluster consisting of 10 open reading frames (dcsA to dcsJ) from Streptomyces lavendulae ATCC 11924 in Escherichia coli. When L-serine and hydroxyurea, the precursors of D-cycloserine, are incubated together with the Escherichia coli resting cell suspension, the cells produce significant amounts of D-cycloserine (350 microM). To increase the productivity, the dcsJ gene, which might be responsible for the excretion, is connected downstream of the four genes, resulting in production of D-cycloserine at 660 microM. To repress the side catalytic activity of DcsD, i.e. the formation of L-cysteine from O-acetylserine and H2S, Escherichia coli chromosomal cysJ and cysK genes, encoding the sulfite reductase alpha subunit and O-acetylserine sulfhydrylase, respectively, are disrupted. The final strain produces 980 microM D-cycloserine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumagai, T.; Koyama, Y.; Oda, K.; Noda, M.; Matoba, Y.; Sugiyama, M.
Molecular cloning and heterologous expression of a biosynthetic gene cluster for the antitubercular agent D-cycloserine produced by Streptomyces lavendulae
Antimicrob. Agents Chemother.
54
1132-1139
2010
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae ATCC 11924 (D2Z027)
brenda
Uda, N.; Matoba, Y.; Kumagai, T.; Oda, K.; Noda, M.; Sugiyama, M
. 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
Antimicrob. Agents Chemother.
57
2603-2612
2013
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae ATCC 11924 (D2Z027)
brenda
Kumagai, T.; Ozawa, T.; Tanimoto, M.; Noda, M.; Matoba, Y.; Sugiyama, M.
High-level heterologous production of D-cycloserine by Escherichia coli
Appl. Environ. Microbiol.
81
7881-7887
2015
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae ATCC 11924 (D2Z027)
brenda
Uda, N.; Matoba, Y.; Oda, K.; Kumagai, T.; Sugiyama, M.
The structural and mutational analyses of O-ureido-L-serine synthase necessary for D-cycloserine biosynthesis
FEBS J.
282
3929-3944
2015
Streptomyces lavendulae (D2Z027), Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924 (D2Z027)
brenda
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