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http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.-.-
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate cofactor; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA cofactor."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2000/01/rdf-schema#comment"Also provides the malonyl groups for polyketide biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://www.w3.org/2004/02/skos/core#prefLabel"[acyl-carrier-protein] S-malonyltransferase"xsd:string
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11373295
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11902724
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10561613
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9208947
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12575934
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11814333
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4561013
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4934182
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5330116
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9914491
http://purl.uniprot.org/enzyme/2.3.1.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9851033