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Literature summary for 1.2.1.50 extracted from

  • Zhu, G.; Shi, X.; Cai, X.
    The reductase domain in a Type i fatty acid synthase from the apicomplexan Cryptosporidium parvum: Restricted substrate preference towards very long chain fatty acyl thioesters (2010), BMC Biochem., 11, 46.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloning of CpFAS1-R domain in a pMAL-c2x vector with maltose binding protein-fusion protein and expression in Escherichia coli Cryptosporidium parvum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
140000
-
recombinant CpFAS1-R domain as maltose binding protein fusion protein, SDS-PAGE Cryptosporidium parvum

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose resin-based chromatography purification Cryptosporidium parvum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain acyl-CoA + NADPH + H+
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Cryptosporidium parvum a long-chain aldehyde + CoA + NADP+
-
?
additional information enzyme only utilizes very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16, enzyme is capable of using NADPH and NADH as electron donors, but prefers NADPH to NADH Cryptosporidium parvum ?
-
?

Synonyms

Synonyms Comment Organism
CpFAS1-R
-
Cryptosporidium parvum

General Information

General Information Comment Organism
metabolism CpFAS1-R enzyme is part of the CpFAS1 multifunctional Type I fatty acid synthase complex with at least 21 enzymatic domains, complex is predicted to function as a fatty acyl elongase preferring long chain fatty acids as substrates Cryptosporidium parvum