http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.-.-.- |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.1.99.- |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.1.-.- |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-[2-(methylsulfanyl)ethyl]hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position."xsd:string |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#comment | "In the enzyme from Sinorhizobium meliloti, Cys-76 is responsible for recognition and proton retrieval of D-isomers, while Cys-181 is responsible for L-isomer recognition and racemization."xsd:string |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme, along with EC 3.5.1.77, EC 3.5.1.87 and EC 3.5.2.2, forms part of the reaction cascade known as the 'hydantoinase process', which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids."xsd:string |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2004/02/skos/core#prefLabel | "hydantoin racemase"xsd:string |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1459947 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/14711700 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17132860 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10949312 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15016445 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11849938 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15784981 |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2004/02/skos/core#altLabel | "5'-monosubstituted-hydantoin racemase"xsd:string |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/5.1.99.5#SIP172DCD1DFF2A5AED |
http://purl.uniprot.org/enzyme/5.1.99.5 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/5.1.99.- |
http://purl.uniprot.org/uniprot/A0A9E8X4M2 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |
http://purl.uniprot.org/uniprot/A0A5E7RVL6 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |
http://purl.uniprot.org/uniprot/A0A0R2EK75 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |
http://purl.uniprot.org/uniprot/A0A5E7IKF9 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |
http://purl.uniprot.org/uniprot/U4Q2U0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |
http://purl.uniprot.org/uniprot/A0A6L5BYA4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.1.99.5 |