Cloning and comparative mapping of a human class III (χ) alcohol dehydrogenase cDNA

A cDNA encoding human class III (χ, ADH5) alcohol dehydrogenase was isolated, sequenced and used to comparatively map this unusual ADH. In their coding sequences, the three major ADH classes were approximately equisimilar, class II and III ADHs sharing the highest sequence identity (67%). A class II...

Full description

Saved in:
Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 164; no. 1; pp. 453 - 460
Main Authors Giri, P.Rathna, Krug, Jane F., Kozak, Christine, Moretti, Tamyra, O'Brien, Stephen J., Seuanez, Hector N., Goldman, David
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 16.10.1989
Elsevier
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:A cDNA encoding human class III (χ, ADH5) alcohol dehydrogenase was isolated, sequenced and used to comparatively map this unusual ADH. In their coding sequences, the three major ADH classes were approximately equisimilar, class II and III ADHs sharing the highest sequence identity (67%). A class III-like ADH was mapped to mouse chromosome 3, site of the ADH gene complex, and synteny of ADH5 with four other ADH loci on human chromosome 4 was confirmed. The nearly full-length 1613 nucleotide cDNA contained 433 nucleotides of 3′ nontranslated sequence and two possible initiation sites for translation. A protein of 374 amino acid residues could be synthesized using the potential initiation codon at nucleotide 59. However, use of the likely initiation codon at nucleotide 5 would produce a protein of 392 residues with 19 additional N-terminal residues as compared to the known protein sequence. The derived protein sequence also differs at residue 166, where Tyr is found. This difference, due to a single base substitution, could result from cloning artifact, polymorphism, or two expressed class III ADH genes.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(89)91741-5