Linked Life Data

234460

Source:http://linkedlifedata.com/resource/pubmed/id/234460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1975-5-21
pubmed:abstractText
Apo-lactic oxidase from Mycobacterium smegmatis reconstituted with the deazaisoalloxazine analogue of FMN, 5-deazaFMN, undergoes reduction by L-lactate but not catalytic reoxidation by O2. The rate of deazaFMN-holo-enzyme reduction by substrate is 1.1 min-1. With L-[alpha-3-H]-lactate, direct tritium transfer to enzyme-bound deazaFMN occurs during reduction. No evidence for a stable covalent lactate-deazaFMN adduct has been obtained. The deaza-FMNH2-enzyme is reoxidized extremely slowly by O2, consistent with the sluggish nonenzymatic reaction of deaza-FMNH2 with oxygen. On the other hand, addition of pyruvate to the deazaFMNH2-enzyme causes rapid reoxidation, a process not detected in the absence of enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1603-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Studies on the mechanism of Mycobacterium smegmatis L-lactate oxidase. 5-Deazaflavin mononucleotide as a coenzyme analogue.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.