Linked Life Data

8672422

Source:http://linkedlifedata.com/resource/pubmed/id/8672422

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1996-8-13
pubmed:abstractText
Energy coupling between ATP hydrolysis and other enzyme reactions requires the phosphorylation of substrate-derived intermediates, or the existence of enzyme-derived intermediates capable of storage and transfer of energy. Salmonella typhimurium nicotinic acid phosphoribosyltransferase (NAPRTase, EC 2.4.2.11) couples net ATP hydrolysis to formation of NAMN and PPi from alpha-PRPP and nicotinic acid [Vinitsky, A., & Grubmeyer, C (1993) J. Biol. Chem. 268, 26004-26010]. In the current work, we have determined that the enzyme reacts with ATP to produce a covalently phosphorylated form of the enzyme (E-P), which is common to both the ATPase and NAMN synthesis functions of NAPRTase. We have isolated E-P and verified its catalytic competence. E-P showed acid lability and base stability, diagnostic of a phosphoramidate linkage. Pyridine and hydroxylamine-catalyzed hydrolysis of E-P gave second-order rate constants consistent with published values for phosphohistidine. Two-dimensional thin-layer chromatography of alkaline-hydrolyzed E-32P showed that the phosphorylated residue co-migrated with authentic 1-phosphohistidine. Chymotrypsin and trypsin proteolysis followed by HPLC and peptide sequencing localized the phosphopeptide to Ala-210 to Phe-222 of the 399-residue protein. This peptide contains a single histidine residue, His-219. NAPRTase phosphorylated at His-219 is an intermediate in the energy transduction mechanism of NAPRTase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3917-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8672422-Adenosine Triphosphatases, pubmed-meshheading:8672422-Adenosine Triphosphate, pubmed-meshheading:8672422-Amino Acid Sequence, pubmed-meshheading:8672422-Animals, pubmed-meshheading:8672422-Binding Sites, pubmed-meshheading:8672422-Cattle, pubmed-meshheading:8672422-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8672422-Enzyme Stability, pubmed-meshheading:8672422-Histidine, pubmed-meshheading:8672422-Humans, pubmed-meshheading:8672422-Kinetics, pubmed-meshheading:8672422-Molecular Sequence Data, pubmed-meshheading:8672422-Pentosyltransferases, pubmed-meshheading:8672422-Peptide Fragments, pubmed-meshheading:8672422-Phosphates, pubmed-meshheading:8672422-Phosphorus Radioisotopes, pubmed-meshheading:8672422-Phosphorylation, pubmed-meshheading:8672422-Salmonella typhimurium, pubmed-meshheading:8672422-Sequence Homology, Amino Acid, pubmed-meshheading:8672422-Substrate Specificity
pubmed:year
1996
pubmed:articleTitle
Energy coupling in Salmonella typhimurium nicotinic acid phosphoribosyltransferase: identification of His-219 as site of phosphorylation.
pubmed:affiliation
Department of Biochemistry and Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't