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Literature summary for 2.3.1.85 extracted from

  • Chakravarty, B.; Gu, Z.; Chirala, S.S.; Wakil, S.J.; Quiocho, F.A.
    Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain (2004), Proc. Natl. Acad. Sci. USA, 101, 15567-15572.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
of thioesterase domain, which comprises two dissimilar subdomains A and B Homo sapiens

Protein Variants

Protein Variants Comment Organism
A2419L 97% reduction of thioesterase activity Homo sapiens
A2419M 92% reduction of thioesterase activity Homo sapiens
F2371W 20% reduction of thioesterase activity Homo sapiens
F2423A 67% reduction of thioesterase activity Homo sapiens
F2423W 24% reduction of thioesterase activity Homo sapiens
I2250W 97% reduction of thioesterase activity Homo sapiens
K2426A 99% reduction of thioesterase activity Homo sapiens
S2422A 7% reduction of thioesterase activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P49327 thioesterase domain of enzyme
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+
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Homo sapiens palmitate + 8 CoA + 7 CO2 + 14 NADP+ + 6 H2O
-
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