| pubmed-article:8024588 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8024588 | lifeskim:mentions | umls-concept:C0085470 | lld:lifeskim |
| pubmed-article:8024588 | lifeskim:mentions | umls-concept:C0019601 | lld:lifeskim |
| pubmed-article:8024588 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:8024588 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8024588 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:8024588 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8024588 | pubmed:dateCreated | 1994-8-1 | lld:pubmed |
| pubmed-article:8024588 | pubmed:abstractText | Site directed mutagenesis was used to investigate the role of Ser-143 in enzyme activity and as a point for attack by cyanide or L-cysteine, two irreversible inhibitors of histidine ammonia-lyase (histidase). Two mutant proteins, a S143A substitution and an A142S-S143A transposition, were made. Both mutant histidases completely lost all enzymatic activity. Western blots with anti-histidase antibodies revealed that the mutant proteins were being expressed at a level equal to that of the wild-type protein. The purified mutant proteins could not incorporate [14C]cyanide nor could they generate the UV-absorbing species normally observed when L-cysteine modifies wild-type histidase. These results support the hypothesis that Ser-143 is the binding site for an as yet unidentified histidase cofactor. | lld:pubmed |
| pubmed-article:8024588 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8024588 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8024588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8024588 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8024588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8024588 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8024588 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8024588 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:8024588 | pubmed:author | pubmed-author:PhillipsA TAT | lld:pubmed |
| pubmed-article:8024588 | pubmed:author | pubmed-author:HernandezDD | lld:pubmed |
| pubmed-article:8024588 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8024588 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:8024588 | pubmed:volume | 201 | lld:pubmed |
| pubmed-article:8024588 | pubmed:geneSymbol | hutH | lld:pubmed |
| pubmed-article:8024588 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8024588 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8024588 | pubmed:pagination | 1433-8 | lld:pubmed |
| pubmed-article:8024588 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:meshHeading | pubmed-meshheading:8024588-... | lld:pubmed |
| pubmed-article:8024588 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8024588 | pubmed:articleTitle | Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida. | lld:pubmed |
| pubmed-article:8024588 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802. | lld:pubmed |
| pubmed-article:8024588 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8024588 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8024588 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8024588 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8024588 | lld:pubmed |
