| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.-.- |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.1.- |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.-.-.- |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "Different forms of the enzyme may have preferences for substrates with different chain length."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0)."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "FabZ, but not FabA, can also accept unsaturated substrates."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme uses fatty acyl thioesters of ACP in vivo."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#prefLabel | "3-hydroxyacyl-[acyl-carrier-protein] dehydratase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8910376 |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7806516 |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2180957 |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4881058 |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] hydro-lyase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "beta-hydroxyoctanoyl-acyl carrier protein dehydrase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "beta-hydroxyoctanoyl thioester dehydratase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "beta-hydroxyoctanoyl-ACP-dehydrase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://www.w3.org/2004/02/skos/core#altLabel | "D-3-hydroxyoctanoyl-[acyl carrier protein] dehydratase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/4.2.1.60 |
| http://purl.uniprot.org/enzyme/4.2.1.59 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/4.2.1.61 |