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Literature summary for 1.3.1.104 extracted from

  • Khare, D.; Hale, W.; Tripathi, A.; Gu, L.; Sherman, D.; Gerwick, W.; Hakansson, K.; Smith, J.
    Structural basis for cyclopropanation by a unique enoyl-acyl carrier protein reductase (2015), Structure, 23, 2213-2223 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Lyngbya majuscula

Protein Variants

Protein Variants Comment Organism
D273A about 55% of wild-type activity Lyngbya majuscula
D273N about 70% of wild-type activity Lyngbya majuscula
K251A activity similar to wild-type Lyngbya majuscula
K251R activity similar to wild-type Lyngbya majuscula
additional information replacement of amino acids 55-66 by CurF enoyl reductase cyclopropanase loop leads to gain-of-function activity as a cyclopropanase. With substrate 3-chloromethyl-crotonyl-[acyl-carrier-protein], the formation of both the reduced product and also the cyclopropanated productis detected at levels of about one-quarter of the total product Lyngbya majuscula

Organism

Organism UniProt Comment Textmining
Lyngbya majuscula Q6E7K0
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-CoA + NADPH + H+
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Lyngbya majuscula butanoyl-CoA + NADP+
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?
gama-chloro-beta-methylcrotonyl-[acyl-carrier-protein] + NADPH + H+
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Lyngbya majuscula gama-chloro-beta-methylbutanoyl-[acyl-carrier-protein] + NADP+
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?

Synonyms

Synonyms Comment Organism
JamJ
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Lyngbya majuscula