| pubmed-article:1540637 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1540637 | lifeskim:mentions | umls-concept:C0009235 | lld:lifeskim |
| pubmed-article:1540637 | lifeskim:mentions | umls-concept:C1417216 | lld:lifeskim |
| pubmed-article:1540637 | lifeskim:mentions | umls-concept:C1149811 | lld:lifeskim |
| pubmed-article:1540637 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1540637 | pubmed:dateCreated | 1992-4-3 | lld:pubmed |
| pubmed-article:1540637 | pubmed:abstractText | Methylmalonate semialdehyde dehydrogenase purified to homogeneity from rat liver possesses, in addition to its coupled aldehyde dehydrogenase and CoA ester synthetic activity, the ability to hydrolyze p-nitrophenyl acetate. The following observations suggest that this activity is an active site phenomenon: (a) p-nitrophenyl acetate hydrolysis was inhibited by malonate semialdehyde, substrate for the dehydrogenase reaction; (b) p-nitrophenyl acetate was a strong competitive inhibitor of the dehydrogenase activity; (c) NAD+ and NADH activated the esterase activity; (d) coenzyme A, acceptor of acyl groups in the dehydrogenase reaction, accelerated the esterase activity; and (e) the product of the esterase reaction proceeding in the presence of coenzyme A was acetyl-CoA. These findings suggest that an S-acyl enzyme (thioester intermediate) is likely common to both the esterase reaction and the aldehyde dehydrogenase/CoA ester synthetic reaction. | lld:pubmed |
| pubmed-article:1540637 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1540637 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1540637 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540637 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1540637 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1540637 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1540637 | pubmed:author | pubmed-author:HarrisR ARA | lld:pubmed |
| pubmed-article:1540637 | pubmed:author | pubmed-author:PopovK MKM | lld:pubmed |
| pubmed-article:1540637 | pubmed:author | pubmed-author:KedishviliN... | lld:pubmed |
| pubmed-article:1540637 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1540637 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:1540637 | pubmed:volume | 1119 | lld:pubmed |
| pubmed-article:1540637 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1540637 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1540637 | pubmed:pagination | 69-73 | lld:pubmed |
| pubmed-article:1540637 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:meshHeading | pubmed-meshheading:1540637-... | lld:pubmed |
| pubmed-article:1540637 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1540637 | pubmed:articleTitle | Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase. | lld:pubmed |
| pubmed-article:1540637 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122. | lld:pubmed |
| pubmed-article:1540637 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1540637 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1540637 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:81708 | entrezgene:pubmed | pubmed-article:1540637 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1540637 | lld:pubmed |
