| pubmed-article:1382 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1382 | lifeskim:mentions | umls-concept:C1265277 | lld:lifeskim |
| pubmed-article:1382 | lifeskim:mentions | umls-concept:C0052331 | lld:lifeskim |
| pubmed-article:1382 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1382 | pubmed:dateCreated | 1976-3-20 | lld:pubmed |
| pubmed-article:1382 | pubmed:abstractText | An arginine decarboxylase has been isolated from a Pseudomonas species. The enzyme is constitutive and did not appear to be repressed by a variety of carbon sources. After an approximately 40-fold purification, the enzyme appeared more similar in its properties to the Escherichia coli biosynthetic arginine decarboxylase than to the E. coli inducible (biodegradative) enzyme. The Pseudomonas arginine decarboxylase exhibited a pH optimum of 8.1 and an absolute requirement of Mg2+ and pyridoxal phosphate, and was inhibited significantly at lower Mg2+ concentrations by the polyamines putrescine, spermidine, and cadaverine. The Km for L-arginine was about 0.25 mM at pH 8.1 AND 7.2. The enzyme was completely inhibited by p-chloromercuribenzoate. The inhibition was prevented by dithiothreitol, a feature that suggests the involvement of an -SH group. Of a variety of labeled amino acids tested, only L-arginine, but not D-arginine was decarboxylated. D-Arginine was a potent inhibitor of arginine decarboxylase with a Ki of 3.2 muM. | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1382 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1382 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1382 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1382 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1382 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:1382 | pubmed:author | pubmed-author:RobertsJJ | lld:pubmed |
| pubmed-article:1382 | pubmed:author | pubmed-author:RosenfeldH... | lld:pubmed |
| pubmed-article:1382 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1382 | pubmed:volume | 125 | lld:pubmed |
| pubmed-article:1382 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1382 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1382 | pubmed:pagination | 601-7 | lld:pubmed |
| pubmed-article:1382 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1382 | pubmed:meshHeading | pubmed-meshheading:1382-Ami... | lld:pubmed |
| pubmed-article:1382 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:1382 | pubmed:articleTitle | Arginine decarboxylase from a Pseudomonas species. | lld:pubmed |
| pubmed-article:1382 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1382 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1382 | lld:pubmed |
