Linked Life Data

7099152

Source:http://linkedlifedata.com/resource/pubmed/id/7099152

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-9-24
pubmed:abstractText
In this paper a steady-state kinetic study on the system lactate dehydrogenase-beta-thiopyruvate-beta-thiolactate is presented and the possible mechanistic and physiological implications are discussed. At pH 7.4 the equilibrium between beta-thiopyruvate and beta-thiolactate, in the presence of NADH and lactate dehydrogenase is largely shifted towards the formation of beta-thiolactate as in the case of pyruvate and lactate. This can can be relevant in connection with the mixed disulfide between cysteine and beta-thiolactate that is observed to be present in the mammalian body fluids. The catalytic mechanism is of the bi-bi compulsory type, and rapid equilibrium conditions for the binding of the first substrate (NADH) are shown to apply. A complex inhibition pattern of inhibitions by both substrates, however, prevents simple suggestions about the nature of the dead-end species involved.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-8177
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
107-12
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Reduction of beta-thiopyruvic acid by lactate dehydrogenase: a kinetic study.
pubmed:publicationType
Journal Article