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Literature summary for 1.2.4.4 extracted from

  • Machius, M.; Wynn, R.M.; Chuang, J.L.; Li, J.; Kluger, R.; Yu, D.; Tomchick, D.R.; Brautigam, C.A.; Chuang, D.T.
    A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase (2006), Structure, 14, 287-298.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of E1b grown in the absence and presence of substrates at 22ΒΊC via the vapor-diffusion method, key tyrosine residue in the E1b active site, functions as a conformational switch to reduce the reactivity of the thiamin diphosphate cofactor, the tyrosine switch further remodels an E1b loop region to promote E1b binding to E2b Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information hE1b-Tyr113Phe mutant, specifically affects the decarboxylation reaction, thiamine diphosphate appears hyperactive, is prone to paracatalytic inactivation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-keto-beta-methylvaleric acid + NADH Homo sapiens
-
?
-
?
alpha-ketoisocaproic acid + NADH Homo sapiens
-
?
-
?
alpha-ketoisovaleric acid + NADH Homo sapiens
-
?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-keto-beta-methylvaleric acid + NADH
-
Homo sapiens ?
-
?
alpha-ketoisocaproic acid + NADH
-
Homo sapiens ?
-
?
alpha-ketoisovaleric acid + NADH
-
Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
BCKDC
-
Homo sapiens
branched-chain alpha-ketoacid dehydrogenase complex
-
Homo sapiens
E1b
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1983
-
alpha-ketoisovaleric acid wild-type Homo sapiens
2.85
-
alpha-ketoisovaleric acid hE1b-Tyr113Phe mutant Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Homo sapiens