http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.1.1.- |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.1.-.- |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#comment | "For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#comment | "In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2)."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#comment | "Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, which acts only on the triglutamate."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#comment | "Reactivation by reductive methylation is catalyzed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II)."xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#prefLabel | "methionine synthase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10978155 |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11731805 |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4946148 |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5799642 |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9548919 |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "5-methyltetrahydrofolate--homocysteine S-methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "cobalamin-dependent methionine synthase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "methionine synthetase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "N(5)-methyltetrahydrofolic--homocysteine vitamin B12 transmethylase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "N(5)-methyltetrahydrofolate methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "methionine synthase (cobalamin-dependent)"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "tetrahydrofolate methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "tetrahydropteroylglutamate methyltransferase"xsd:string |
http://purl.uniprot.org/enzyme/2.1.1.13 | http://www.w3.org/2004/02/skos/core#altLabel | "tetrahydropteroylglutamic methyltransferase"xsd:string |