| pubmed-article:7547974 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7547974 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:7547974 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:7547974 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:7547974 | lifeskim:mentions | umls-concept:C0069240 | lld:lifeskim |
| pubmed-article:7547974 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:7547974 | pubmed:dateCreated | 1995-11-6 | lld:pubmed |
| pubmed-article:7547974 | pubmed:abstractText | The pH dependence of kinetic parameters using natural and alternative reactants was determined in order to obtain information on the chemical mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase (OASS) from Salmonella typhimurium. A general mechanism is proposed for OASS in which OAS binds with its alpha-amine unprotonated to carry out a nucleophilic attack on C4' of the protonated Schiff base and with the acetyl carbonyl hydrogen-bonded to a protonated enzyme group (or a water molecule), which aids in the beta-elimination of acetate. The enzyme lysine that was in Schiff base linkage with the active site pyridoxal 5'-phosphate deprotonates the alpha-carbon in the beta-elimination reaction, and a proton is likely released with the acetate product. Sulfide likely binds as HS- to undergo nucleophilic attack on the alpha-aminoacrylate intermediate, followed by protonation of the alpha-carbon by the enzyme lysine. In OASS-A, HS- is hydrogen-bonded to the enzyme group that assists in the beta-elimination of acetate, but this is not the case for OASS-B. The pH independent equilibrium constant for the first half-reaction of OASS-A is 1.6 x 10(-3), while the second half-reaction is practically irreversible. | lld:pubmed |
| pubmed-article:7547974 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7547974 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7547974 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7547974 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7547974 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7547974 | pubmed:author | pubmed-author:CookP FPF | lld:pubmed |
| pubmed-article:7547974 | pubmed:author | pubmed-author:JacobsonT MTM | lld:pubmed |
| pubmed-article:7547974 | pubmed:author | pubmed-author:TaiC HCH | lld:pubmed |
| pubmed-article:7547974 | pubmed:author | pubmed-author:SimmonsJ... | lld:pubmed |
| pubmed-article:7547974 | pubmed:author | pubmed-author:NalaboluS RSR | lld:pubmed |
| pubmed-article:7547974 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7547974 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:7547974 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:7547974 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7547974 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7547974 | pubmed:pagination | 12311-22 | lld:pubmed |
| pubmed-article:7547974 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7547974 | pubmed:meshHeading | pubmed-meshheading:7547974-... | lld:pubmed |
| pubmed-article:7547974 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7547974 | pubmed:articleTitle | Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. | lld:pubmed |
| pubmed-article:7547974 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of North Texas Health Sciences Center, Fort Worth 76107, USA. | lld:pubmed |
| pubmed-article:7547974 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7547974 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7547974 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7547974 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
