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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aminotransferase, cysteine, CGT, cysteine aminotransferase, L-cysteine aminotransferase, L-cysteine-2-oxoglutarate aminotransferase, More,
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aminotransferase, cysteine
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cysteine aminotransferase
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L-cysteine aminotransferase
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L-cysteine-2-oxoglutarate aminotransferase
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additional information
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cytosolic cysteine aminotransferase, EC 2.6.1.3, is identical with cytosolic aspartate aminotransferase, EC 2.6.1.1
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L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate
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amino group transfer
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L-cysteine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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L-alanine 3-sulfinic acid + 2-oxoglutarate
pyruvate 3-sulfinic acid + L-glutamate
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at pH 8.0
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?
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
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?
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
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r
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
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important part of enzyme together with beta-mercaptopyruvate sulfurtransferase in the regulation of thiosulfate formation
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?
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L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
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r
L-cysteine + 2-oxoglutarate
L-glutamate + beta-mercaptopyruvate
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important part of enzyme together with beta-mercaptopyruvate sulfurtransferase in the regulation of thiosulfate formation
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?
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pyridoxal 5'-phosphate
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pyridoxal phosphate protein
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alpha-Methyl-DL-cysteine
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inhibits transamination of cysteine
sodium phosphate buffer
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Carcinoma, Ehrlich Tumor
Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.
Hypothyroidism
SULPHUR-CONTAINING AMINO ACIDS METABOLISM IN EXPERIMENTAL HYPER- AND HYPOTHYROIDISM IN RATS.
Neoplasms
Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer.
Neoplasms
Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.
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7 - 11
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about 60% of activity maximum at pH 7 and 11
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brenda
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dorsal root ganglion
brenda
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brenda
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peripheral neuron
brenda
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pheochromocytoma-derived cell
brenda
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brenda
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physiological function
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cystathionine beta-synthase, cysteine aminotransferase, and mercaptopyruvate sulfurtransferase, but not cystathionine gamma-lyase, are expressed in PC12 cells and the dorsal root ganglion, and appreciable amounts of H2S are produced from L-cysteine in the presence of alpha-ketoglutarate, together with dithiothreitol. The production of H2S is inhibited by cysteine aminotransferase inhibitor aminooxyacetic acid, and competitive cysteine aminotransferase substrates L-aspartate and oxaloacetate. The amount of H2S produced by cysteine aminotransferase/mercaptopyruvate sulfurtransferase at pH 8.0, a physiological mitochondrial matrix pH, is comparable to that produced by cystathionine beta-synthase and cystathionine beta-synthase in the liver and the brain, respectively
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AATC_HUMAN
413
0
46248
Swiss-Prot
other Location (Reliability: 3 )
AATC_MACFA
413
0
46393
Swiss-Prot
other Location (Reliability: 3 )
AATC_MOUSE
413
0
46248
Swiss-Prot
other Location (Reliability: 4 )
AATC_PANTR
413
0
46233
Swiss-Prot
other Location (Reliability: 3 )
AATC_PIG
413
0
46475
Swiss-Prot
other Location (Reliability: 4 )
AATC_PONAB
413
0
46213
Swiss-Prot
other Location (Reliability: 3 )
AATC_RABIT
31
0
3427
Swiss-Prot
other Location (Reliability: 3 )
AATC_RAT
413
0
46429
Swiss-Prot
other Location (Reliability: 5 )
AATC_BOVIN
413
0
46399
Swiss-Prot
other Location (Reliability: 4 )
AATC_CHICK
412
0
45935
Swiss-Prot
other Location (Reliability: 5 )
AATC_HORSE
413
0
46345
Swiss-Prot
other Location (Reliability: 4 )
Q0K213_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
406
0
43720
TrEMBL
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84000
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1 * 84000, SDS-PAGE
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monomer
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1 * 84000, SDS-PAGE
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additional information
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1 h at room temperature, complete inactivation
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-20ºC, 68% inactivated after 32 days
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TEAE-cellulose, isoelectric focusing
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Thibert, R.J.; Schmidt, D.E.
Purification and partial characterization of cysteine-glutamate transaminase from rat liver
Can. J. Biochem.
55
958-964
1977
Rattus norvegicus
brenda
Akagi, R.
Purification and characterization of cysteine aminotransferase from rat liver cytosol
Acta Med. Okayama
36
187-197
1982
Rattus norvegicus
brenda
Miyamoto, R.; Otsuguro, K.; Yamaguchi, S.; Ito, S.
Contribution of cysteine aminotransferase and mercaptopyruvate sulfurtransferase to hydrogen sulfide production in peripheral neurons
J. Neurochem.
130
29-40
2014
Rattus norvegicus
brenda
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2.6.1.3 cysteine transaminase
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