|Title||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.|
|Publication Type||Journal Article|
|Year of Publication||1989|
|Authors||von der Osten, CH, Barbas, CF, Wong, CH, Sinskey, AJ|
|Date Published||1989 Nov|
|Keywords||Amino Acid Sequence, Base Sequence, Cloning, Molecular, Corynebacterium, DNA, Bacterial, Fructose-Bisphosphate Aldolase, Genes, Bacterial, Glucose, Molecular Sequence Data, Restriction Mapping, Transcription, Genetic|
The Corynebacterium glutamicum fda gene encoding fructose-1,6-biphosphate (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 37,092 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 II 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.
|Alternate Journal||Mol Microbiol|