Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae

Journal Article · Sat Jul 01 00:00:00 EDT 1989 · Journal of Bacteriology; (USA)

OSTI ID:5025812

Conway, T ^[1]; Ingram, L O ^[2]

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1. Univ. of Nebraska, Lincoln (USA)
2. Univ. of Florida, Gainesville (USA)

The gene that encodes 1,2-propanediol oxidoreductase (fucO) from Escherichia coli was sequenced. The reading frame specified a protein of 383 amino acids (including the N-terminal methionine), with an aggregate molecular weight of 40,642. The induction of fucO transcription, which occurred in the presence of fucose, was confirmed by Northern blot analysis. In E. coli, the primary fucO transcript was approximately 2.1 kilobases in length. The 5{prime} end of the transcript began more than 0.7 kilobase upstream of the fucO start codon within or beyond the fucA gene. Propanediol oxidoreductase exhibited 41.7% identity with the iron-containing alcohol dehydrogenase II from Zymomonas mobilis and 39.5% identity with ADH4 from Saccharomyces cerevisiae. These three proteins did not share homology with either short-chain or long-chain zinc-containing alcohol dehydrogenase enzymes. We propose that these three unusual alcohol dehydrogenases define a new family of enzymes.

• DOE Contract Number: FG05-86ER13575
• OSTI ID: 5025812
• Journal Information: Journal of Bacteriology; (USA), Vol. 171:7; ISSN 0021-9193
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ESCHERICHIA COLI
MOLECULAR BIOLOGY
OXIDOREDUCTASES
DNA SEQUENCING
SACCHAROMYCES CEREVISIAE
ENZYME ACTIVITY
ZYMOMONAS MOBILIS
ALCOHOL DEHYDROGENASE
AMINO ACID SEQUENCE
COMPARATIVE EVALUATIONS
TRANSCRIPTION
BACTERIA
ENZYMES
EUMYCOTA
FUNGI
HEMIACETAL DEHYDROGENASES
MICROORGANISMS
MOLECULAR STRUCTURE
PLANTS
SACCHAROMYCES
STRUCTURAL CHEMICAL ANALYSIS
YEASTS
550400* - Genetics