| pubmed-article:15317500 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15317500 | lifeskim:mentions | umls-concept:C1151515 | lld:lifeskim |
| pubmed-article:15317500 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15317500 | pubmed:dateCreated | 2004-8-19 | lld:pubmed |
| pubmed-article:15317500 | pubmed:abstractText | Nalpha-Acetylated microperoxidase-8 (Ac-MP-8) is a water soluble, ferric heme model for peroxidases. We report here that Ac-MP-8 catalyzes catalase-type reaction in addition to peroxidase-type and cytochrome P450-type reactions. The catalase activity of Ac-MP-8 was determined by the Clark oxygen electrode, which measures the production of oxygen in solution. The Km and kcat of the decomposition of hydrogen peroxide (H2O2) catalyzed by Ac-MP-8 are 40.9 mm and 4.1 per s, respectively. The specificity constant (kcat/Km) of Ac-MP-8 in catalase-type reaction of H2O2 is 100.2,/m/s, which is 5- to 12- and 50- to 100-fold less than those of MPs in cytochrome P450-type reaction of aniline/H2O2 and peroxidase-type reaction of o-methoxyphenol/H2O2, respectively. These results indicate that Ac-MP-8 can catalyze three different types of reactions, and the relative catalytic specificities of Ac-MP-8 with a histidyl ligand exhibit the following orders: peroxidase-type > cytochrome P450-type > catalase-type reactions. Comparisons of the enzyme activities of Ac-MP-8 suggest that the fifth ligands of hemoproteins influence the ratio of the three types of reactions. | lld:pubmed |
| pubmed-article:15317500 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15317500 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15317500 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15317500 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15317500 | pubmed:issn | 1397-002X | lld:pubmed |
| pubmed-article:15317500 | pubmed:author | pubmed-author:ChuangW-JWJ | lld:pubmed |
| pubmed-article:15317500 | pubmed:author | pubmed-author:SANYJJ | lld:pubmed |
| pubmed-article:15317500 | pubmed:author | pubmed-author:JengW-YWY | lld:pubmed |
| pubmed-article:15317500 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15317500 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:15317500 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15317500 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15317500 | pubmed:pagination | 104-9 | lld:pubmed |
| pubmed-article:15317500 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:meshHeading | pubmed-meshheading:15317500... | lld:pubmed |
| pubmed-article:15317500 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15317500 | pubmed:articleTitle | The catalase activity of Nalpha-acetyl-microperoxidase-8. | lld:pubmed |
| pubmed-article:15317500 | pubmed:affiliation | Department of Biochemistry and Institute of Basic Medical Sciences, National Cheng Kung University Medical College, Tainan 701, Taiwan. | lld:pubmed |
| pubmed-article:15317500 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15317500 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:15317500 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15317500 | lld:pubmed |
