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Literature summary for 1.2.1.80 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
Search for more literature for 1.2.1.80

Application

Application Comment Organism
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)

Cloned (Comment) Organism
in a Rosetta bacterial strain serving as an expression host for the maltose-binding protein-CpFAS1-R fusion protein Cryptosporidium parvum

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Cryptosporidium parvum
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
-
 Cryptosporidium parvum fatty aldehyde + acyl-carrier protein + NAD(P)+
-
 ?
hexacosanoyl-CoA + NAD(P)H + H+
-
 Cryptosporidium parvum hexacosanal + CoA + NAD(P)+
-
 ?
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

Synonyms Comment Organism
CpFAS1 acyl reductase
-
 Cryptosporidium parvum
CpFAS1-R
-
 Cryptosporidium parvum

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Cryptosporidium parvum
NADPH preferred cofactor Cryptosporidium parvum

General Information

General Information Comment Organism
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