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 (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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.91 | - |
hexacosanoyl-CoA | pH 7.2, temperature not specified in the publication | Cryptosporidium parvum |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Cryptosporidium parvum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
to homogeneity as a maltose-binding protein-fusion protein by amylose-resin based affinity chromatography | Cryptosporidium parvum |
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 | Comment | Organism |
---|---|---|
CpFAS1 acyl reductase | - |
Cryptosporidium parvum |
CpFAS1-R | - |
Cryptosporidium parvum |
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 | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Cryptosporidium parvum | |
NADPH | preferred cofactor | Cryptosporidium parvum |
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 |