| pubmed-article:9132 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9132 | lifeskim:mentions | umls-concept:C0022938 | lld:lifeskim |
| pubmed-article:9132 | lifeskim:mentions | umls-concept:C0019605 | lld:lifeskim |
| pubmed-article:9132 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:9132 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9132 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:9132 | pubmed:dateCreated | 1976-11-21 | lld:pubmed |
| pubmed-article:9132 | pubmed:abstractText | Two classes of sulfhydryl groups in histidine decarboxylase from Lactobacillus 30 a can be differentiated by their reaction with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). Five cysteinyl residues (class I) of the native enzyme are titrated by DTNB as the pH of the reaction medium is increased from 6.5 to 7.5; the pH-rate profile for their reaction is described by a pKa of 9.2. An additional five thiol groups (class II) are titrated only when denaturing agents are added above neutral pH. Histidine decarboxylase is completely inactivated by DTNB in a kinetically second-order process (Kapp = 660 +/- 20 M-1 min-1 at pH 7.6 and 25 degrees C) which occurs coincident with and at the same rate as modification of the five class-I SH groups of the enzyme, i.e., one thiol group per pyruvoyl prosthetic group. The competitive inhibitors, histamine and imidazole, markedly enhanced the reactivity of these cysteinyl residues toward DTNB; this enhancement is accompanied by a concomitant increase in the rate of inactivation. A single SH group in each of the five catalytic units of histidine decarboxylase is thus implicated as being critical for the expression of enzymatic activity. | lld:pubmed |
| pubmed-article:9132 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9132 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9132 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9132 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9132 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9132 | pubmed:author | pubmed-author:SnellE EEE | lld:pubmed |
| pubmed-article:9132 | pubmed:author | pubmed-author:LaneR SRS | lld:pubmed |
| pubmed-article:9132 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9132 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:9132 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:9132 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9132 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9132 | pubmed:pagination | 4175-9 | lld:pubmed |
| pubmed-article:9132 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-His... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Hyd... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Imi... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Car... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Gua... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Kin... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Lac... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Pro... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Bin... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Bin... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-His... | lld:pubmed |
| pubmed-article:9132 | pubmed:meshHeading | pubmed-meshheading:9132-Dit... | lld:pubmed |
| pubmed-article:9132 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:9132 | pubmed:articleTitle | Histidine decarboxylase of Lactobacillus 30a: function and reactivity of sulfhydryl groups. | lld:pubmed |
| pubmed-article:9132 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9132 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
