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Kynurenine—oxoglutarate transaminase

From Wikipedia, the free encyclopedia
kynurenine-oxoglutarate transaminase
Kynurenine aminotransferase-I homodimer, Human
Identifiers
EC no.2.6.1.7
CAS no.9030-38-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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Inenzymology, akynurenine-oxoglutarate transaminase (EC2.6.1.7) is anenzyme thatcatalyzes thechemical reaction

L-kynurenine + 2-oxoglutarate ⇌ 4-(2-aminophenyl)-2,4-dioxobutanoate +L-glutamate

Thus, the twosubstrates of this enzyme areL-kynurenine and2-oxoglutarate, whereas its twoproducts are4-(2-aminophenyl)-2,4-dioxobutanoate andL-glutamate. The former product is an unstable α-oxo acid that quickly undergoes intramolecular cyclization to formkynurenic acid.[1]

This enzyme belongs to the family oftransferases, to be specific, thetransaminases, that transfer nitrogenous groups. Thesystematic name of this enzyme class isL-kynurenine:2-oxoglutarate aminotransferase. Other names in common use includekynurenine transaminase (cyclizing),kynurenine 2-oxoglutarate transaminase,kynurenine aminotransferase, andL-kynurenine aminotransferase. This enzyme participates intryptophan metabolism. It employs onecofactor,pyridoxal phosphate.

KYAT1,AADAT (aka KYAT2), andKYAT3 are examples of enzymes of this class.GOT2 (aka KYAT4) is also believed to catalyze the above reaction.[2]

Structural studies

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As of early 2009, 18structures have been solved for this class of enzymes, withPDB accession codes1X0M,1YIY,1YIZ,1W7L,1W7M,1W7N,3E2F,3E2Y,3E2Z,2ZJG,2YGZ,2Z61,2R5C,2R2N,2R5E,3B46,3DC1, and2QLN.

References

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  1. ^Han Q, Cai T, Tagle DA, Robinson H, Li J (August 2008)."Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II".Bioscience Reports.28 (4):205–15.doi:10.1042/BSR20080085.PMC 2559858.PMID 18620547.
  2. ^Guidetti P, Amori L, Sapko MT, Okuno E, Schwarcz R (July 2007). "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain".Journal of Neurochemistry.102 (1):103–11.doi:10.1111/j.1471-4159.2007.04556.x.PMID 17442055.S2CID 20413002.

Further reading

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2.6.1:Transaminases
2.6.3: Oximinotransferases
2.6.99: Other
Activity
Regulation
Classification
Kinetics
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