Linked Life Data

2059626

Source:http://linkedlifedata.com/resource/pubmed/id/2059626

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1991-8-2
pubmed:abstractText
Carboxy-terminal amidation is a prevalent posttranslational modification necessary for the bioactivity of many neurohormonal peptides. We recently reported that in addition to peptidylglycine alpha-monooxygenase (PAM), a second enzyme, which we now call peptidylamidoglycolate lyase (PGL), functions in the enzymatic formation of amides [Katopodis et al. (1990) Biochemistry 29, 4551]. The monooxygenase first catalyzes formation of the alpha-hydroxyglycine derivative of the glycine-extended precursor, and the lyase subsequently catalyzes breakdown of the PAM product to the amidated peptide and glyoxylate. We report here the first primary sequence data for PGL, which establish that it is part of the putative protein precursor which also contains PAM. We also show that PAM and PGL activities are colocalized in the secretory granular fraction of neurointermediate pituitary as would be expected for enzymes sharing the same precursor. Time course studies of the amidation reaction using purified soluble pituitary PAM and PGL indicate that both enzymes are essential for enzymatic amidation. Finally, PGL has no effect on the substrate or inhibition kinetics of PAM, and purified pituitary PAM has an acidic pH optimum consistent with its known localization in secretory granules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6189-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Functional and structural characterization of peptidylamidoglycolate lyase, the enzyme catalyzing the second step in peptide amidation.
pubmed:affiliation
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta 30332.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't