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Information on EC 2.5.1.48 - cystathionine gamma-synthase

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EC Tree
IUBMB Comments
A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
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This record set is specific for:
UNIPROT: A0PKT3
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cystathionine gamma-synthase, cystathionine synthase, atcgs, cystathionine synthetase, cystathionine-gamma-synthase, o-succinylhomoserine synthetase, o-succinylhomoserine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CGS
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CS,26
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cystathionine synthase
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cystathionine synthetase
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cystathionine-gamma-synthase
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homoserine O-transsuccinylase
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homoserine transsuccinylase
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O-succinyl-L-homoserine succinate-lyase (adding cysteine)
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O-succinylhomoserine (Thiol)-lyase
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O-succinylhomoserine synthase
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O-succinylhomoserine synthetase
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synthase, cystathionine gamma-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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gamma-replacement
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SYSTEMATIC NAME
IUBMB Comments
O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase
A pyridoxal-phosphate protein. Also reacts with hydrogen sulfide and methanethiol as replacing agents, producing homocysteine and methionine, respectively. In the absence of thiol, can also catalyse beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-70-0
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0PKT3_MYCUA
Mycobacterium ulcerans (strain Agy99)
388
0
40723
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.9 A resolution. Cofactor pyridoxal 5'-phosphate binds tightly to Lys208 with a covalent-bond length ranging between 1.3 and 1.4 A. The cofactor is stabilized by a series of hydrogen bonds from Gly86, Met87, Asn158, Asp183 and Ser205 from one monomer and Tyr56 and Arg58 from the second monomer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clifton, M.C.; Abendroth, J.; Edwards, T.E.; Leibly, D.J.; Gillespie, A.K.; Ferrell, M.; Dieterich, S.H.; Exley, I.; Staker, B.L.; Myler, P.J.; Van Voorhis, W.C.; Stewart, L.J.
Structure of the cystathionine gamma-synthase MetB from Mycobacterium ulcerans
Acta Crystallogr. Sect. F
67
1154-1158
2011
Mycobacterium ulcerans (A0PKT3), Mycobacterium ulcerans Agy99 (A0PKT3)
Manually annotated by BRENDA team