| pubmed-article:17134376 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17134376 | lifeskim:mentions | umls-concept:C0040329 | lld:lifeskim |
| pubmed-article:17134376 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:17134376 | lifeskim:mentions | umls-concept:C0072500 | lld:lifeskim |
| pubmed-article:17134376 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17134376 | lifeskim:mentions | umls-concept:C1704788 | lld:lifeskim |
| pubmed-article:17134376 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17134376 | pubmed:dateCreated | 2007-2-22 | lld:pubmed |
| pubmed-article:17134376 | pubmed:abstractText | PPO (protoporphyrinogen IX oxidase) catalyses the flavin-dependent six-electron oxidation of protogen (protoporphyrinogen IX) to form proto (protoporphyrin IX), a crucial step in haem and chlorophyll biosynthesis. The apparent K(m) value for wild-type tobacco PPO2 (mitochondrial PPO) was 1.17 muM, with a V(max) of 4.27 muM.min(-1).mg(-1) and a catalytic activity k(cat) of 6.0 s(-1). Amino acid residues that appear important for substrate binding in a crystal structure-based model of the substrate docked in the active site were interrogated by site-directed mutagenesis. PPO2 variant F392H did not reveal detectable enzyme activity indicating an important role of Phe(392) in substrate ring A stacking. Mutations of Leu(356), Leu(372) and Arg(98) increased k(cat) values up to 100-fold, indicating that the native residues are not essential for establishing an orientation of the substrate conductive to catalysis. Increased K(m) values of these PPO2 variants from 2- to 100-fold suggest that these residues are involved in, but not essential to, substrate binding via rings B and C. Moreover, one prominent structural constellation of human PPO causing the disease variegate porphyria (N67W/S374D) was successfully transferred into the tobacco PPO2 background. Therefore tobacco PPO2 represents a useful model system for the understanding of the structure-function relationship underlying detrimental human enzyme defects. | lld:pubmed |
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| pubmed-article:17134376 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17134376 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17134376 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17134376 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17134376 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17134376 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17134376 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:Messerschmidt... | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:KochMichaelM | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:JahnDieterD | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:JahnMartinaM | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:MasoumiAvaA | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:HeinemannIlka... | lld:pubmed |
| pubmed-article:17134376 | pubmed:author | pubmed-author:DiekmannNinaN | lld:pubmed |
| pubmed-article:17134376 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17134376 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17134376 | pubmed:volume | 402 | lld:pubmed |
| pubmed-article:17134376 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17134376 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17134376 | pubmed:pagination | 575-80 | lld:pubmed |
| pubmed-article:17134376 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
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| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:meshHeading | pubmed-meshheading:17134376... | lld:pubmed |
| pubmed-article:17134376 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17134376 | pubmed:articleTitle | Functional definition of the tobacco protoporphyrinogen IX oxidase substrate-binding site. | lld:pubmed |
| pubmed-article:17134376 | pubmed:affiliation | Institute of Microbiology, Technical University Braunschweig, Spielmannstr. 7, 38106 Braunschweig, Germany. | lld:pubmed |
| pubmed-article:17134376 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17134376 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17134376 | lld:pubmed |
