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
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.
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-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)
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
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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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
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
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
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
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
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2.6.99.3 O-ureido-L-serine synthase
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