| http://purl.uniprot.org/citations/3110154 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3110154 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3110154 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/3110154 | http://www.w3.org/2000/01/rdf-schema#comment | "Pyruvate:NADP+ oxidoreductase was homogeneously purified from crude extract of Euglena gracilis. The Mr of the enzyme was estimated to be 309,000 by gel filtration. The enzyme migrated as a single protein band with Mr of 166,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that the enzyme consists of two identical polypeptides. The absorption spectrum of the native enzyme exhibited maxima at 278, 380, and 430 nm, and a broad shoulder was observed around 480 nm; the maximum at 430 nm was eliminated by reduction of the enzyme with dithionite. Reduction of the enzyme with pyruvate and CoA and reoxidation with NADP+ were proved from changes of absorption spectra. The enzyme contained 2 molecules of FAD and 8 molecules of iron. It was also indicated that the enzyme was thiamine pyrophosphate-dependent. The enzyme was oxygen-sensitive, and the reaction was affected by the presence of oxygen. Pyruvate was the most active substrate, but the enzyme was slightly active for 2-oxobutyrate, 3-hydroxypyruvate, and oxalacetate, but not for glyoxylate and 2-oxoglutarate. The native electron acceptor was NADP+, whereas NAD+ was completely inactive. Methyl viologen, benzyl viologen, FAD, and FMN were utilized as artificial electron acceptors, whereas spinach and Clostridium ferredoxins were inactive. Pyruvate synthesis by reductive carboxylation of acetyl-CoA with NADPH as the electron donor occurred by the reverse reaction of the enzyme. The enzyme also catalyzed a pyruvate-CO2 exchange reaction and electron-transfer reaction from NADPH to other electron acceptors like methyl viologen. These results indicate that pyruvate:NADP+ oxidoreductase in E. gracilis is clearly distinct from either the pyruvate dehydrogenase multienzyme complex or pyruvate:ferredoxin oxidoreductase."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)48057-x"xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)48057-x"xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Nakano Y."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Nakano Y."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Ono K."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Ono K."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Inui H."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Inui H."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Kitaoka S."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Kitaoka S."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Miyatake K."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/author | "Miyatake K."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/pages | "9130-9135"xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/pages | "9130-9135"xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/title | "Purification and characterization of pyruvate:NADP+ oxidoreductase in Euglena gracilis."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/title | "Purification and characterization of pyruvate:NADP+ oxidoreductase in Euglena gracilis."xsd:string |
| http://purl.uniprot.org/citations/3110154 | http://purl.uniprot.org/core/volume | "262"xsd:string |