http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.-.- |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.3.1.- |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://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/2.3.1.39 | http://www.w3.org/2000/01/rdf-schema#comment | "Also provides the malonyl groups for polyketide biosynthesis."xsd:string |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://www.w3.org/2004/02/skos/core#prefLabel | "[acyl-carrier-protein] S-malonyltransferase"xsd:string |
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http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11902724 |
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http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9208947 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12575934 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11814333 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4561013 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4934182 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5330116 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9914491 |
http://purl.uniprot.org/enzyme/2.3.1.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9851033 |