Information on EC 2.6.99.3 - O-ureido-L-serine synthase

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The expected taxonomic range for this enzyme is: Streptomyces lavendulae

EC NUMBER
COMMENTARY hide
2.6.99.3
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RECOMMENDED NAME
GeneOntology No.
O-ureido-L-serine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydroxyurea = O-ureido-L-serine + acetate
show the reaction diagram
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
D-cycloserine biosynthesis
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydroxyurea
O-ureido-L-serine + acetate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9 - 18
Hydroxyurea
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6 - 11
Hydroxyurea
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 1.2
Hydroxyurea
850
0.15
O-acetyl-L-serine
Streptomyces lavendulae
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30°C, pH 8.0, cosubstrate: hydroxyurea
680
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
activity increases from pH 5.0 to pH 9.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
activity at pH 7.5 is about 45% compared to activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
4 * 36000, SDS-PAGE
126000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
S121M
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
V74T
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97F
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97M
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decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis