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Molecular cloning, nucleotide sequence and fine‐structural analysis of the Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum fructose‐1,6‐biphosphate aldolase to class I and class II aldolases
Author(s) -
Osten C. H.,
Barbas C. F.,
Wong C.H.,
Sinskey A. J.
Publication year - 1989
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1989.tb00148.x
Subject(s) - corynebacterium glutamicum , biology , gene , nucleic acid sequence , genetics , corynebacterium , structural gene , molecular cloning , cloning (programming) , aldolase a , sequence (biology) , nucleotide , sequence analysis , biochemistry , peptide sequence , enzyme , escherichia coli , bacteria , computer science , programming language
Summary The Corynebacterium glutamicum fda gene encoding fructose‐ 1,6‐btphosphate (FBP) aldolase has been isolated by complementation of an Escherichia coli mutant. The nucleotide sequence of a 3371 bp chromosomal fragment containing the C. glutamicum fda gene was determined. The N‐terminal amino acid sequence of C. glutamicum FBP aldolase identified the correct initiation site for the fda gene, and a molecular weight of 37092 was predicted for the fda polypeptide. S1 nuclease mapping identified the transcriptional start site, and Northern hybridization analysis indicated that the fda gene encodes a single 1.3 kb transcript. The primary structure of C. glutamicum FBP aldolase shows strong homology to class 11 FBP aldolases. Conservation of primary structure was observed between class I and class II aldolases, but several residues essential for catalytic activity in class I aldolases were absent from class II aldolases.