Linked Life Data

3571231

Source:http://linkedlifedata.com/resource/pubmed/id/3571231

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1987-6-5
pubmed:abstractText
L-Lactate-2-monooxygenase (EC 1.13.12.4) inactivated by 1-fluoro-2,4-dinitrobenzene essentially as described previously (Choong, Y. S., Shepherd, M. G., and Sullivan, P. A. (1978) Biochem. J. 173, 255-262) incorporated 2.8 mol of the dinitrophenyl (DNP) moiety per mole of flavin. The inhibitors 2-methyl lactate or sulfite decreased the incorporation to 0.9 mol of DNP per mole of flavin. Peptide mapping by high performance liquid chromatography of radioactively labeled protein digested with trypsin showed three peaks of radioactivity. DNP-amino acid analysis and peptide sequencing showed that 2 distinct cysteine residues and a histidine residue had been modified. Both cysteine peptides were protected from modification by either of the inhibitors, whereas the histidine was only partially protected. The sum of the 2 cysteine peptides accounted for nearly 1 mole of label per mole of monomer. Since both of the cysteines are protected by inhibitors, they both must be in or near the substrate-binding site of the enzyme and appear to be modified in a mutually exclusive fashion. The histidine, on the other hand, does not lie directly in the substrate-binding site. It is possible that this histidine is the positively charged residue that is postulated to be near the N-1 position of the flavin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5705-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
L-lactate-2-monooxygenase. Sequence of peptides containing residues modified by 1-fluoro-2,4-dinitrobenzene.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't