Isolation and sequence analysis of the pmi gene encoding phosphomannose isomerase of Streptococcus mutans.
A gene encoding a phosphomannose isomerase from Streptococcus mutans GS-5 was identified immediately downstream from the fructokinase gene, scrK. Nucleotide sequence analysis of this region revealed an open reading frame (ORF) specifying a putative protein of 316 amino acids. The gene cloned in Escherichia coli expressed strong phosphomannose isomerase activity. The deduced amino acid sequence of the pmi gene has no significant similarity with any of the previously reported phosphomannose isomerase enzymes. Insertional inactivation of the upstream gene, scrK, in S. mutans also drastically reduced phosphomannose isomerase activity and the ability of the organism to utilize mannose as a sole carbon source. These results suggest that the S. mutans pmi gene constitutes an operon with the scrK gene.
Sato
Y
Y
Department of Biochemistry, Tokyo Dental College, Chiba City, Japan.
Yamamoto
Y
Y
Kizaki
H
H
Kuramitsu
H K
HK
D000595:Amino Acid Sequence; D001419:Bacteria / Q000235:genetics; D001483:Base Sequence; D004269:DNA, Bacterial / Q000302:isolation & purification; D005798:Genes, Bacterial / Q000235:genetics*; D008359:Mannose-6-Phosphate Isomerase / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D016366:Open Reading Frames; D015183:Restriction Mapping; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013295:Streptococcus mutans / Q000201:enzymology / Q000235:genetics*
D004269:DNA, Bacterial; D008359:Mannose-6-Phosphate Isomerase