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Information on EC 6.3.3.5 - O-ureido-D-serine cyclo-ligase
for references in articles please use BRENDA:EC6.3.3.5
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.3 Cyclo-ligases
6.3.3.5 O-ureido-D-serine cyclo-ligase
IUBMB Comments
The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.
The expected taxonomic range for this enzyme is: Streptomyces lavendulae
showSynonyms
DcsG, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DcsG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-ureido-D-serine + ATP + H2O = D-cycloserine + CO2 + NH3 + ADP + phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-cycloserine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
O-ureido-D-serine cyclo-ligase (D-cycloserine-forming)
The enzyme participates in the biosynthetic pathway of D-cycloserine, an antibiotic substance produced by several Streptomyces species.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + NH3 + ADP + phosphate
Substrates: -
Products: -
Products: -
?
beta-aminooxy-D-alanine + ATP + H2O
D-cycloserine + ?
Substrates: -
Products: -
Products: -
?
beta-aminooxy-D-alanine + ATP + H2O
D-cycloserine + ?
Substrates: -
Products: -
Products: -
?
D-2,4-diaminobutyrate + ATP + H2O
?
Substrates: -
Products: -
Products: -
?
D-2,4-diaminobutyrate + ATP + H2O
?
Substrates: -
Products: -
Products: -
?
D-homocysteine + ATP + H2O
?
Substrates: -
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: the enzyme is involved in the biosynthesis of the antituberculosis antibiotic D-cycloserine
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: O-ureido-D-serine i.e. (2R)-2-amino-3-[(carbamoylamino)oxy]propanoate
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: O-ureido-D-serine i.e. (2R)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O-ureido-L-serine
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: O-ureido-D-serine i.e. (2R)-2-amino-3-[(carbamoylamino)oxy]propanoate
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: the enzyme is involved in the biosynthesis of the antituberculosis antibiotic D-cycloserine
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: O-ureido-D-serine i.e. (2R)-2-amino-3-[(carbamoylamino)oxy]propanoate. No activity with O-ureido-L-serine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + NH3 + ADP + phosphate
Substrates: -
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: the enzyme is involved in the biosynthesis of the antituberculosis antibiotic D-cycloserine
Products: -
Products: -
?
O-ureido-D-serine + ATP + H2O
D-cycloserine + CO2 + ammonia + ADP + phosphate
Substrates: the enzyme is involved in the biosynthesis of the antituberculosis antibiotic D-cycloserine
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
DcsG catalyzes specifically the generation of an intramolecular covalent bond
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C142A
mutation reduces the activity of the three substrates investigated by 25% to 60%
E271A
mutation reduces the activity of the three substrates investigated by more than 95%
E271Q
mutation reduces the activity of the three substrates investigated by more than 95%
K202A
mutation reduces the activity of the three substrates investigated by more than 95%
P215A
mutation reduces the activity of the three substrates investigated by about 90%
R220A
mutation reduces the activity of the three substrates investigated by about 90%
R254A
mutation reduces the activity of the three substrates investigated by more than 95%
S276A
mutation reduces the activity of the three substrates investigated by 50 to 90%
W57A
mutation reduces the activity of the three substrates investigated by more than 95%
Y143A
mutation reduces the activity of the three substrates investigated by 70 to 95%
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally His6-tagged enzyme is overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
expression of four D-cycloserine biosynthetic genes (dcsC, dcsD, dcsE, and dcsG) in tandem in Escherichia coli. In presence of L-serine and hydroxyurea, D-cycloserine is produced. Coexpression of gene DcsJ and optimization of conditions results in production of 0.98 mM D-cycloserine
synthesis
-
expression of four D-cycloserine biosynthetic genes (dcsC, dcsD, dcsE, and dcsG) in tandem in Escherichia coli. In presence of L-serine and hydroxyurea, D-cycloserine is produced. Coexpression of gene DcsJ and optimization of conditions results in production of 0.98 mM 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 (D2Z030), Streptomyces lavendulae ATCC 11924 (D2Z030)
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 (D2Z030), Streptomyces lavendulae ATCC 11924 (D2Z030)
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 (D2Z030), Streptomyces lavendulae ATCC 11924 (D2Z030)
brenda
Matoba, Y.; Uda, N.; Kudo, M.; Sugiyama, M.
Cyclization mechanism catalyzed by an ATP-grasp enzyme essential for D-cycloserine biosynthesis
FEBS J.
287
2763-2778
2020
Streptomyces lavendulae (D2Z030)
brenda
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