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Information on EC 4.4.1.1 - cystathionine gamma-lyase

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EC Tree
IUBMB Comments
A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
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UNIPROT: Q5H4T8
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Synonyms
cystathionine gamma-lyase, cystathionase, gamma-cystathionase, cystathionine-gamma-lyase, cs-like, cysteine desulfhydrase, l-cysteine desulfhydrase, cystalysin, cystathionine gamma lyase, prb-ra, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cystathionine gamma-lyase-like protein
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cystalysin
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cystathionase
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cystathioninase
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cystathionine gamma-lyase
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cysteine desulfhydrase
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cysteine lyase
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cystine desulfhydrase
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dehydratase, homoserine
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desulfhydrase, cysteine
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gamma-CTL
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gamma-cystathionase
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homoserine deaminase
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homoserine deaminase-cystathionase
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homoserine dehydratase
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lyase, cystathionine gamma-
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PRB-RA
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Probasin-related antigen
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SYSTEMATIC NAME
IUBMB Comments
L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)
A multifunctional pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-96-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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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?
Q5H4T8_XANOR
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
397
0
42586
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of two different shapes, plate-shaped and pyramid-shaped, diffract to 2.9 and 3.2 A resolution and belong to the primitive orthogonal space group P212121 and the tetragonal space group P41 (or P43), with unit-cell parameters a = 73.0, b = 144.9, c = 152.3 A and a = b = 78.2, c = 300.7 A, respectively. For the P212121 crystals, three or four monomers exist in the asymmetric unit with a corresponding VM of 3.02 or 2.26 A3/Da and a solvent content of 59.3 or 45.7%. For the P41 (or P43) crystals, four or five monomers exist in the asymmetric unit with a corresponding VM of 2.59 or 2.09 A3/Da and a solvent content of 52.5 or 40.6%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
enzyme is an antibacterial drug-target protein against Xanthomonas oryzae pv. oryzae. Bacterial blight caused by Xanthomonas oryzae pv. oryzae is the most destructive bacterial disease of rice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ngo, P.T.; Kim, J.K.; Kim, H.; Jung, J.; Ahn, Y.J.; Kim, J.G.; Lee, B.M.; Kang, H.W.; Kang, L.W.
Expression, crystallization and preliminary X-ray crystallographic analysis of XometC, a cystathionine gamma-lyase-like protein from Xanthomonas oryzae pv. oryzae
Acta Crystallogr. Sect. F
64
750-753
2008
Xanthomonas oryzae pv. oryzae (Q5H4T8), Xanthomonas oryzae pv. oryzae
Manually annotated by BRENDA team