| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.11.1.- |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.11.-.- |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "Two types of lipoyl-dependent peroxiredoxins have been reported from bacteria."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "The second type, which has been characterized in Xylella fastidiosa, consists of only one type of subunit, which interacts directly with lipoylated proteins."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "AhpD is reduced in turn by lipoylated proteins."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "In that system, AhpC catalyzes reduction of the substrate, resulting in an intramolecular disulfide."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid)."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "AhpD then forms an intermolecular disulfide cross-link with AhpC, reducing it back to active state."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2000/01/rdf-schema#comment | "One type is the AhpC/AhpD system, originally described from Mycobacterium tuberculosis."xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://www.w3.org/2004/02/skos/core#prefLabel | "lipoyl-dependent peroxiredoxin"xsd:string |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10766746 |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12761216 |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15178486 |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16368957 |
| http://purl.uniprot.org/enzyme/1.11.1.28 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/20463026 |