N-terminal acetylation in a third protein family of vertebrae alcohol dehydrogenase/retinal reductase found through a 'proteomics' approach in enzymecharacterization

Citation
D. Hirschberg et al., N-terminal acetylation in a third protein family of vertebrae alcohol dehydrogenase/retinal reductase found through a 'proteomics' approach in enzymecharacterization, CELL MOL L, 58(9), 2001, pp. 1323-1326
Citations number
9
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
58
Issue
9
Year of publication
2001
Pages
1323 - 1326
Database
ISI
SICI code
1420-682X(200108)58:9<1323:NAIATP>2.0.ZU;2-Z
Abstract
A recent finding of a novel class of retinol-active alcohol dehydrogenase ( ADH) in frog prompted analysis of this activity in other vertebrate forms. Surprisingly, yet another and still more unrelated ADH was identified in ch icken tissues. It was found to be a member of the aldo-keto reductase (AKR) enzyme family, not previously known as an ADH in vertebrates. Its terminal blocking group and the N-terminal segment, not assigned by protein and cDN A structure analysis, were determined by electrospray tandem mass spectrome try after protein isolation by two-dimensional gel electrophoresis. The N t erminus is Acetyl-Ala- and the N-terminal segment contains two consecutive Asn residues. The results establish the new ADH enzyme of the AKR family an d show the usefulness of combined gel separation and mass spectrometry in e nzyme characterization.