Information on EC 2.6.1.75 - cysteine-conjugate transaminase

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The expected taxonomic range for this enzyme is: Rattus norvegicus

EC NUMBER
COMMENTARY hide
2.6.1.75
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RECOMMENDED NAME
GeneOntology No.
cysteine-conjugate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate = S-(4-bromophenyl)mercaptopyruvate + L-glutamate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase
A number of cysteine conjugates can also act.
CAS REGISTRY NUMBER
COMMENTARY hide
117698-05-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CAT-1 partially purified, obtained with isoenzymes CAT-IIA, CAT-IIB
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartic acid + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
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reactivity of isozymes: less than 5% for CAT-I, 15% for CAT-IIA, 42% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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-
?
L-cysteine sulfinic acid + 2-oxoglutarate
2-oxo-3-sulfinopropionate + L-glutamate
show the reaction diagram
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reactivity of isozymes: less than 5% for CAT-I, 7% for CAT-IIA, 76% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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?
L-kynurenine + 2-oxoglutarate
L-glutamate + 4-(2-aminophenyl)-2,4-dioxobutanoate
show the reaction diagram
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reactivity of isozymes: 7% for CAT-I, 6% for CAT-IIA, 12% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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-
?
S-(1-butyl)-L-cysteine + 2-oxoglutarate
S-(1-butyl)-3-thiopyruvate + L-glutamate
show the reaction diagram
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reactivity of isozymes: 23% for CAT-I, 30% for CAT-IIA, 33% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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?
S-(1-propyl)-L-cysteine + 2-oxoglutarate
S-(1-propyl)-3-thiopyruvate + L-glutamate
show the reaction diagram
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reactivity of isozymes: 16% for CAT-I, 13% for CAT-IIA, 14% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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?
S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate
S-(4-bromophenyl)-3-thiopyruvate + L-glutamate
show the reaction diagram
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highest activity with all three isoenzymes: CAT-I, CAT-IIA, CAT-IIB
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r
S-(4-bromophenyl)-L-cysteine + 4-methylsulfanyl-2-oxobutanoate
S-(4-bromophenyl)-3-thiopyruvate + methionine
show the reaction diagram
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21% of activity compared to 2-oxoglutarate
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?
S-benzyl-L-cysteine + 2-oxoglutarate
S-benzyl-3-thiopyruvate + L-glutamate
show the reaction diagram
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reactivity of isozymes: 19% for CAT-I, 16% for CAT-IIA, 20% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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?
S-phenyl-L-cysteine + 2-oxoglutarate
S-phenyl-3-thiopyruvate + L-glutamate
show the reaction diagram
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reactivity of isozymes: 36% for CAT-I, 24% for CAT-IIA, 34% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine
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?
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
S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate
S-(4-bromophenyl)-3-thiopyruvate + L-glutamate
show the reaction diagram
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highest activity with all three isoenzymes: CAT-I, CAT-IIA, CAT-IIB
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r
additional information
?
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isoenzyme CAT-I may be involved in in vivo transamination of cysteine conjugates in rat liver, value of reverse reaction is 5 times lower than forward reaction by CAT-I, forward and reverse reaction at similar rates for CAT-IIA and CAT-IIB
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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may be a coenzyme, indicated by inhibitory effects of carbonyl reagents
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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slight stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aminooxyacetic acid
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1 mM, complete inhibition of the three isoenzymes
EDTA
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1 mM, 92% remaining activity
hydroxylamine
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1 mM, complete inhibition of the three isoenzymes
KCN
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1 mM, 38% remaining activity for CAT 1, less efficient inhibitor for CAT-IIA and CAT-IIB
MgCl2
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1 mM, 90% remaining activity
additional information
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iodoacetic acid and dithiothreitol, at 1 mM concentration, are poor inhibitors
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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slight stimulation, 117% of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 1.33
2-oxoglutarate
0.67 - 2
S-(4-Bromophenyl)-L-cysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.263
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isoenzyme CAT-IIB, pH 7.0, 35C
0.297
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isoenzyme CAT-IIA, pH 7.0, 35C
0.423
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isoenzyme CAT-I, pH 7.0, 35C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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isoenzymes CAT-I, CAT-IIA, CAT-IIB
additional information
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most active in Tris-acetate buffer, other buffers inhibit enzyme activity by 50-90% in comparison with this buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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64% of transaminase activity in cytosol
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
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CAT-IIA, CAT-IIB have the same molecular weight, all of them determined by gel filtration; isoenzyme CAT-I
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of pyridoxal 5'-phosphate is essential for activity after ammonium sulfate fractionation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 200 mM phosphate buffer pH 7.4, 50% loss of activity in two weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate partial purification, followed by DEAE-cellulose, where it is separated from CAT IIa and CAT-IIB, later on, hydroxyapatite column and gel filtration steps
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