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Literature summary for 3.1.3.52 extracted from

  • White, P.J.; McGarrah, R.W.; Grimsrud, P.A.; Tso, S.C.; Yang, W.H.; Haldeman, J.M.; Grenier-Larouche, T.; An, J.; Lapworth, A.L.; Astapova, I.; Hannou, S.A.; George, T.; Arlotto, M.; Olson, L.B.; Lai, M.; Zhang, G.F.; Ilkayeva, O.; Herman, M.A.; Wynn, R.M.; Chuang, D.T.; Newgard, C.B.
    The BCKDH kinase and phosphatase integrate BCAA and lipid metabolism via regulation of ATP-citrate lyase (2018), Cell Metab., 27, 1281-1293 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus D4A7X5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] phosphate + H2O
-
 Rattus norvegicus [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)] + phosphate
-
 ?
[ATP-citrate lyase] phosphate + H2O
-
 Rattus norvegicus [ATP-citrate lyase] + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PPM1K
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function inhibition of the kinase BDK or overexpression of the phosphatase PPM1K that regulate branched-chain ketoacid dehydrogenase BCKDH, lowers circulating branched-chain amino acid levels, reduces hepatic steatosis, and improves glucose tolerance in the absence of weight loss in Zucker fatty rats. ATP-citrate lyase is an alternate substrate of BDK and PPM1K. BDK and PPM1K transcript levels are increased and repressed, respectively, in response to fructose feeding or expression of the ChREBP-b transcription factor Rattus norvegicus