Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12

Melibiose uptake and hydrolysis in E.coli is performed by the MelB and MelA proteins, respectively. We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also...

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Bibliographic Details
Published in:Nucleic acids research 1987-03, Vol.15 (5), p.2213-2220
Main Authors: Liljestoüm, Pirkko L., Liljestrom, Peter
Format: Article
Language:English
Subjects:
alpha-Galactosidase - genetics
Amino Acid Sequence
Bacteriology
Base Sequence
Biological and medical sciences
Cloning, Molecular
Codon
DNA Restriction Enzymes
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Galactosidases - genetics
Genes
Genes, Bacterial
Genetic Complementation Test
Genetics
Microbiology
Molecular Weight
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Summary:Melibiose uptake and hydrolysis in E.coli is performed by the MelB and MelA proteins, respectively. We report the cloning and sequencing of the melA gene. The nucleotide sequence data showed that melA codes for a 450 amino acid long protein with a molecular weight of 50.6 kd. The sequence data also supported the assumption that the mel locus forms an operon with melA in proximal position. A comparison of MelA with alpha-galactosidase proteins from yeast and human origin showed that these proteins have only limited homology, the yeast and human proteins being more related. However, regions common to all three proteins were found indicating sequences that might comprise the active site of alpha-galactosidase.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/15.5.2213