| pubmed-article:8580849 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0002594 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0085732 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C1323252 | lld:lifeskim |
| pubmed-article:8580849 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:8580849 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8580849 | pubmed:dateCreated | 1996-3-15 | lld:pubmed |
| pubmed-article:8580849 | pubmed:abstractText | Of the major amino acid side chains that anchor pyridoxal 5'-phosphate at the coenzyme binding site of bacterial D-amino acid transaminase, two have been substituted using site-directed mutagenesis. Thus, Ser-180 was changed to an Ala (S180A) with little effect on enzyme activity, but replacement of Tyr-31 by Gln (Y31Q) led to 99% loss of activity. Titration of SH groups of the native Y31Q enzyme with DTNB proceeded much faster and to a greater extent than the corresponding titration for the native wild-type and S180A mutant enzymes. The stability of each mutant to denaturing agents such as urea or guanidine was similar, i.e., in their PLP forms, S180A and Y31Q lost 50% of their activities at a 5-15% lower concentration of urea or guanidine than did the wild-type enzyme. Upon removal of denaturing agent, significant activity was restored in the absence of added pyridoxal 5'-phosphate, but addition of thiols was required. In spite of its low activity, Y31Q was able to form the PMP form of the enzyme just as readily as the wild-type and the S180A enzymes in the presence of normal D-amino acid substrates. However, beta-chloro-D-alanine was a much better substrate and inactivator of the Y31Q enzyme than it was for the wild-type or S180A enzymes, most likely because the Y31Q mutant formed the pyridoxamine 5-phosphate form more rapidly than the other two enzymes. The stereochemical fidelity of the Y31Q recombinant mutant enzyme was much less than that of the S180A and wild-type enzymes because racemase activity, i.e., conversion of L-alanine to D-alanine, was higher than for the wild-type or S180A mutant enzymes, perhaps because the coenzyme has more flexibility in this mutant enzyme. | lld:pubmed |
| pubmed-article:8580849 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8580849 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8580849 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8580849 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8580849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8580849 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8580849 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8580849 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:SodaKK | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:ManningJ MJM | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:RingeDD | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:Van OphemP... | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:PetskoGG | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:PospischilM... | lld:pubmed |
| pubmed-article:8580849 | pubmed:author | pubmed-author:PeisachDD | lld:pubmed |
| pubmed-article:8580849 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8580849 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:8580849 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8580849 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8580849 | pubmed:pagination | 2578-86 | lld:pubmed |
| pubmed-article:8580849 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8580849 | pubmed:meshHeading | pubmed-meshheading:8580849-... | lld:pubmed |
| pubmed-article:8580849 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8580849 | pubmed:articleTitle | Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding. | lld:pubmed |
| pubmed-article:8580849 | pubmed:affiliation | Rockefeller University, New York, New York, USA. | lld:pubmed |
| pubmed-article:8580849 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8580849 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
