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Literature summary 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

Application

EC Number Application Comment Organism
1.2.1.80 drug development since the giant CpFAS1 and polyketide synthase CpPKS1 are structurally and functionally different from human Type I FAS, these parasite megasynthases may serve as novel drug targets, also because CpFAS1 and CpPKS1 utilize R domains to release final products Cryptosporidium parvum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.50 cloning of CpFAS1-R domain in a pMAL-c2x vector with maltose binding protein-fusion protein and expression in Escherichia coli Cryptosporidium parvum
1.2.1.80 in a Rosetta bacterial strain serving as an expression host for the maltose-binding protein-CpFAS1-R fusion protein Cryptosporidium parvum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.80 0.91
-
 hexacosanoyl-CoA pH 7.2, temperature not specified in the publication Cryptosporidium parvum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.50 140000
-
 recombinant CpFAS1-R domain as maltose binding protein fusion protein, SDS-PAGE Cryptosporidium parvum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.80 fatty acyl-[acyl-carrier protein] + NAD(P)H + H+ Cryptosporidium parvum
-
 fatty aldehyde + acyl-carrier protein + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.50 Cryptosporidium parvum
-
-
-
1.2.1.80 Cryptosporidium parvum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.50 amylose resin-based chromatography purification Cryptosporidium parvum
1.2.1.80 to homogeneity as a maltose-binding protein-fusion protein by amylose-resin based affinity chromatography Cryptosporidium parvum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.50 a long-chain acyl-CoA + NADPH + H+
-
 Cryptosporidium parvum a long-chain aldehyde + CoA + NADP+
-
 ?
1.2.1.50 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 ?
-
 ?
1.2.1.80 fatty acyl-CoA + NAD(P)H + H+ CpFAS1-R can only utilize very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16 or fewer carbons Cryptosporidium parvum fatty aldehyde + CoA + NAD(P)+ since aldehydes are toxic to cells it is very likely that the fatty aldehyde is immediately transformed into the corresponding alcohol by the enzyme complex ?
1.2.1.80 fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
-
 Cryptosporidium parvum fatty aldehyde + acyl-carrier protein + NAD(P)+
-
 ?
1.2.1.80 hexacosanoyl-CoA + NAD(P)H + H+
-
 Cryptosporidium parvum hexacosanal + CoA + NAD(P)+
-
 ?
1.2.1.80 additional information because of technical difficulties in preparing the native substrates for CpFAS1-R, which are very long chain fatty acyl-ACPs, long chain and very long chain fatty acyl-CoAs are used as substrates to assay CpFAS1-R activity Cryptosporidium parvum ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.50 CpFAS1-R
-
 Cryptosporidium parvum
1.2.1.80 CpFAS1 acyl reductase
-
 Cryptosporidium parvum
1.2.1.80 CpFAS1-R
-
 Cryptosporidium parvum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.80 0.077
-
 hexacosanoyl-CoA pH 7.2, temperature not specified in the publication Cryptosporidium parvum

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.80 NADH
-
 Cryptosporidium parvum
1.2.1.80 NADPH preferred cofactor Cryptosporidium parvum

General Information

EC Number General Information Comment Organism
1.2.1.50 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
1.2.1.80 metabolism C-terminal CpFAS1-R enzyme belongs to a multifunctional Type I fatty acid synthase, CpFAS1, with at least 21 enzymatic domains, this megasynthase is predicted to function as a fatty acyl elongase Cryptosporidium parvum