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Literature summary extracted from

  • Tomisawa, H.; Ichimoto, N.; Takanohashi, Y.; Ichihara, S.; Fukazawa, H.; Tateishi, M.
    Purification and characterization of cysteine conjugate transaminases from rat liver (1988), Xenobiotica, 18, 1015-1028.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.6.1.75 N-ethylmaleimide slight stimulation, 117% of activity Rattus norvegicus

General Stability

EC Number General Stability Organism
2.6.1.75 addition of pyridoxal 5'-phosphate is essential for activity after ammonium sulfate fractionation Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.75 aminooxyacetic acid 1 mM, complete inhibition of the three isoenzymes Rattus norvegicus
2.6.1.75 EDTA 1 mM, 92% remaining activity Rattus norvegicus
2.6.1.75 hydroxylamine 1 mM, complete inhibition of the three isoenzymes Rattus norvegicus
2.6.1.75 KCN 1 mM, 38% remaining activity for CAT 1, less efficient inhibitor for CAT-IIA and CAT-IIB Rattus norvegicus
2.6.1.75 MgCl2 1 mM, 90% remaining activity Rattus norvegicus
2.6.1.75 additional information iodoacetic acid and dithiothreitol, at 1 mM concentration, are poor inhibitors Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.75 0.41
-
2-oxoglutarate isoenzyme CAT-IIA, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 0.5
-
2-oxoglutarate isoenzyme CAT-IIB, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 0.67
-
S-(4-Bromophenyl)-L-cysteine isoenzyme CAT-IIA, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 1
-
S-(4-Bromophenyl)-L-cysteine isoenzyme CAT-I, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 1.33
-
2-oxoglutarate isoenzyme CAT-I, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 2
-
S-(4-Bromophenyl)-L-cysteine isoenzyme CAT-IIB, pH 7.0, 35°C Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.75 cytosol 64% of transaminase activity in cytosol Rattus norvegicus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.6.1.75 Ca2+ slight stimulation Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.75 64000
-
isoenzyme CAT-I Rattus norvegicus
2.6.1.75 64000
-
CAT-IIA, CAT-IIB have the same molecular weight, all of them determined by gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.75 additional information Rattus norvegicus 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 ?
-
?
2.6.1.75 S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate Rattus norvegicus highest activity with all three isoenzymes: CAT-I, CAT-IIA, CAT-IIB S-(4-bromophenyl)-3-thiopyruvate + L-glutamate
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.75 Rattus norvegicus
-
CAT-1 partially purified, obtained with isoenzymes CAT-IIA, CAT-IIB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.75 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 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.75 liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.75 0.263
-
isoenzyme CAT-IIB, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 0.297
-
isoenzyme CAT-IIA, pH 7.0, 35°C Rattus norvegicus
2.6.1.75 0.423
-
isoenzyme CAT-I, pH 7.0, 35°C Rattus norvegicus

Storage Stability

EC Number Storage Stability Organism
2.6.1.75 -20°C, 200 mM phosphate buffer pH 7.4, 50% loss of activity in two weeks Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.75 L-aspartic acid + 2-oxoglutarate 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 Rattus norvegicus oxaloacetate + L-glutamate
-
?
2.6.1.75 L-cysteine sulfinic acid + 2-oxoglutarate 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 Rattus norvegicus 2-oxo-3-sulfinopropionate + L-glutamate
-
?
2.6.1.75 L-kynurenine + 2-oxoglutarate reactivity of isozymes: 7% for CAT-I, 6% for CAT-IIA, 12% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine Rattus norvegicus L-glutamate + 4-(2-aminophenyl)-2,4-dioxobutanoate
-
?
2.6.1.75 additional information 2-oxobutanoate, 2-oxosuccinate and pyruvate exhibit about 3% of activity compared to alpha-ketoglutarate Rattus norvegicus ?
-
?
2.6.1.75 additional information glyoxylic acid, S-ethyl-L-cysteine, S-2-propyl-L-cysteine, S-cyclohexyl-L-cysteine, S-(2-chloroethyl)-L-cysteine, S-phenyl-L-cysteine sulfoxide are not substrates, negligible activity with other amino acids e.g. L-leucine, L-configuration is essential Rattus norvegicus ?
-
?
2.6.1.75 additional information 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 Rattus norvegicus ?
-
?
2.6.1.75 S-(1-butyl)-L-cysteine + 2-oxoglutarate reactivity of isozymes: 23% for CAT-I, 30% for CAT-IIA, 33% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine Rattus norvegicus S-(1-butyl)-3-thiopyruvate + L-glutamate
-
?
2.6.1.75 S-(1-propyl)-L-cysteine + 2-oxoglutarate reactivity of isozymes: 16% for CAT-I, 13% for CAT-IIA, 14% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine Rattus norvegicus S-(1-propyl)-3-thiopyruvate + L-glutamate
-
?
2.6.1.75 S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate highest activity with all three isoenzymes: CAT-I, CAT-IIA, CAT-IIB Rattus norvegicus S-(4-bromophenyl)-3-thiopyruvate + L-glutamate
-
r
2.6.1.75 S-(4-bromophenyl)-L-cysteine + 4-methylsulfanyl-2-oxobutanoate 21% of activity compared to 2-oxoglutarate Rattus norvegicus S-(4-bromophenyl)-3-thiopyruvate + methionine
-
?
2.6.1.75 S-benzyl-L-cysteine + 2-oxoglutarate reactivity of isozymes: 19% for CAT-I, 16% for CAT-IIA, 20% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine Rattus norvegicus S-benzyl-3-thiopyruvate + L-glutamate
-
?
2.6.1.75 S-phenyl-L-cysteine + 2-oxoglutarate reactivity of isozymes: 36% for CAT-I, 24% for CAT-IIA, 34% for CAT-IIB, activity compared to S-(4-bromophenyl)-L-cysteine Rattus norvegicus S-phenyl-3-thiopyruvate + L-glutamate
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.75 37
-
assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.75 additional information
-
most active in Tris-acetate buffer, other buffers inhibit enzyme activity by 50-90% in comparison with this buffer Rattus norvegicus
2.6.1.75 7
-
isoenzymes CAT-I, CAT-IIA, CAT-IIB Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.75 pyridoxal 5'-phosphate may be a coenzyme, indicated by inhibitory effects of carbonyl reagents Rattus norvegicus