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Nucleotide sequence of the gene encoding the Corynebacterium glutamicum mannose enzyme II and analyses of the deduced protein sequence
Author(s) -
Lee JungKee,
Sung MoonHee,
Yoon KiHong,
Yu JuHyun,
Oh TaeKwang
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06880.x
Subject(s) - corynebacterium glutamicum , nucleic acid sequence , biology , biochemistry , peptide sequence , homology (biology) , mannose , enzyme , gene , microbiology and biotechnology , escherichia coli , cyclic nucleotide binding domain
Abstract The complete nucleotide sequence of the gene encoding the Corynebacterium glutamicum mannose enzyme II (EII Man ) was determined. The gene consisted of 2052 base pairs encoding a protein of 683 amino acid residues; the molecular mass of the protein subunit was calculated to be 72570 Da. The N‐terminal hydrophilic domain of EII Man showed 39.7% homology with a C‐terminal hydrophilic domain of Escherichia coli glucose‐specific enzyme II (EII Glc ). Similar homology was shown between the C‐terminal sequence of EII Man and the E. coli glucose‐specific enzyme III (EIII Glc ), or the EIII‐like domain of Streptococcus mutans sucrose‐specific enzyme II. Sequence comparison with other EIIs showed that EII Man contained residues His‐602 and Cys‐28 which were homologous to the potential phosphorylation sites of EIII Glc , or EIII‐like domains, and hydrophilic domains (IIB) of several EIIs, respectively.

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