| pubmed-article:12686138 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C0066319 | lld:lifeskim |
| pubmed-article:12686138 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:12686138 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:12686138 | pubmed:dateCreated | 2003-4-10 | lld:pubmed |
| pubmed-article:12686138 | pubmed:abstractText | Methylamine dehydrogenase (MADH) possesses an alpha(2)beta(2) subunit structure with each smaller beta subunit possessing a tryptophan tryptophylquinone (TTQ) prosthetic group. Phe(55) of the alpha subunit is located where the substrate channel from the enzyme surface opens into the active site. Site-directed mutagenesis studies have revealed several roles for this residue in catalysis and electron transfer (ET) by MADH. Site-directed mutagenesis of either alpha Phe(55) or beta Ile(107) (a residue in the beta subunit which interacts with alpha Phe(55)) converts MADH into enzymes with specificities for long-chain amines, amylamine or propylamine. Mutation of alpha Phe(55) also affects monovalent cation binding to the active site. alpha F55A MADH exhibits an increased K(d) for cation-dependent spectral changes and a decreased K(d) for cation-dependent stimulation of the rate of gated ET from N-quinol MADH to amicyanin. These results demonstrate that alpha Phe(55) is able to directly participate in a wide range of biochemical processes not typically observed for a phenylalanine residue. | lld:pubmed |
| pubmed-article:12686138 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12686138 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12686138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12686138 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12686138 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12686138 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:12686138 | pubmed:author | pubmed-author:DavidsonVicto... | lld:pubmed |
| pubmed-article:12686138 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12686138 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:12686138 | pubmed:volume | 1647 | lld:pubmed |
| pubmed-article:12686138 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12686138 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12686138 | pubmed:pagination | 230-3 | lld:pubmed |
| pubmed-article:12686138 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:meshHeading | pubmed-meshheading:12686138... | lld:pubmed |
| pubmed-article:12686138 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12686138 | pubmed:articleTitle | Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55. | lld:pubmed |
| pubmed-article:12686138 | pubmed:affiliation | Department of Biochemistry, The University of Mississippi Medical Center, 2500 N. State Street, Jackson, MS 39216-4505, USA. vdavidson@biochem.umsmed.edu | lld:pubmed |
| pubmed-article:12686138 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12686138 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12686138 | pubmed:publicationType | Review | lld:pubmed |
