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Title: Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): Sequence comparison and expression in Escherichia coli

Abstract

Zymomonas mobilis ferments sugars to produce ethanol with two biochemically distinct isoenzymes of alcohol dehydrogenase. The adhA gene encoding alcohol dehydrogenase I has now been sequenced and compared with the adhB gene, which encodes the second isoenzyme. The deduced amino acid sequences for these gene products exhibited no apparent homology. Alcohol dehydrogenase I contained 337 amino acids, with a subunit molecular weight of 36,096. Based on comparisons of primary amino acid sequences, this enzyme belongs to the family of zinc alcohol dehydrogenases which have been described primarily in eucaryotes. Nearly all of the 22 strictly conserved amino acids in this group were also conserved in Z. mobilis alcohol dehydrogenase I. Alcohol dehydrogenase I is an abundant protein, although adhA lacked many of the features previously reported in four other highly expressed genes from Z. mobilis. Codon usage in adhA is not highly biased and includes many codons which were unused by pdc, adhB, gap, and pgk. The ribosomal binding region of adhA lacked the canonical Shine-Dalgarno sequence found in the other highly expressed genes from Z. mobilis. Although these features may facilitate the expression of high enzyme levels, they do not appear to be essential for the expression of Z.more » mobilis adhA.« less

Authors:
; ; ;  [1]
  1. Univ. of Florida, Gainesville (USA)
Publication Date:
OSTI Identifier:
6534222
DOE Contract Number:  
FG05-86ER13575
Resource Type:
Journal Article
Journal Name:
Journal of Bacteriology; (USA)
Additional Journal Information:
Journal Volume: 172:5; Journal ID: ISSN 0021-9193
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ALCOHOL DEHYDROGENASE; GENES; AMINO ACID SEQUENCE; BIOSYNTHESIS; DNA-CLONING; ESCHERICHIA COLI; ETHANOL; ZYMOMONAS MOBILIS; ALCOHOLS; BACTERIA; CLONING; DNA HYBRIDIZATION; ENZYMES; HEMIACETAL DEHYDROGENASES; HYBRIDIZATION; HYDROXY COMPOUNDS; MICROORGANISMS; MOLECULAR STRUCTURE; ORGANIC COMPOUNDS; OXIDOREDUCTASES; SYNTHESIS; 550200* - Biochemistry

Citation Formats

Keshav, K F, Yomano, L P, An, Haejung, and Ingram, L O. Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): Sequence comparison and expression in Escherichia coli. United States: N. p., 1990. Web.
Keshav, K F, Yomano, L P, An, Haejung, & Ingram, L O. Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): Sequence comparison and expression in Escherichia coli. United States.
Keshav, K F, Yomano, L P, An, Haejung, and Ingram, L O. 1990. "Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): Sequence comparison and expression in Escherichia coli". United States.
@article{osti_6534222,
title = {Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): Sequence comparison and expression in Escherichia coli},
author = {Keshav, K F and Yomano, L P and An, Haejung and Ingram, L O},
abstractNote = {Zymomonas mobilis ferments sugars to produce ethanol with two biochemically distinct isoenzymes of alcohol dehydrogenase. The adhA gene encoding alcohol dehydrogenase I has now been sequenced and compared with the adhB gene, which encodes the second isoenzyme. The deduced amino acid sequences for these gene products exhibited no apparent homology. Alcohol dehydrogenase I contained 337 amino acids, with a subunit molecular weight of 36,096. Based on comparisons of primary amino acid sequences, this enzyme belongs to the family of zinc alcohol dehydrogenases which have been described primarily in eucaryotes. Nearly all of the 22 strictly conserved amino acids in this group were also conserved in Z. mobilis alcohol dehydrogenase I. Alcohol dehydrogenase I is an abundant protein, although adhA lacked many of the features previously reported in four other highly expressed genes from Z. mobilis. Codon usage in adhA is not highly biased and includes many codons which were unused by pdc, adhB, gap, and pgk. The ribosomal binding region of adhA lacked the canonical Shine-Dalgarno sequence found in the other highly expressed genes from Z. mobilis. Although these features may facilitate the expression of high enzyme levels, they do not appear to be essential for the expression of Z. mobilis adhA.},
doi = {},
url = {https://www.osti.gov/biblio/6534222}, journal = {Journal of Bacteriology; (USA)},
issn = {0021-9193},
number = ,
volume = 172:5,
place = {United States},
year = {Tue May 01 00:00:00 EDT 1990},
month = {Tue May 01 00:00:00 EDT 1990}
}