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J. Biol. Chem., Vol. 266, Issue 36, 24287-24294, Dec, 1991
K Watanabe, K Chishiro, K Kitamura and Y Suzuki
The gene encoding for an extremely thermostable oligo-1,6-glucosidase from
Bacillus thermoglucosidasius KP1006 (DSM2542, obligate thermophile) was
sequenced. The amino acid sequence deduced from the nucleotide sequence of
the gene (1686 base pairs) corresponded to a protein of 562 amino acid
residues with a Mr of 66,502. Its predicted amino acid composition, Mr, and
N-terminal sequence of 12 residues were consistent with those determined
for B. thermoglucosidasius oligo-1,6- glucosidase. The deduced sequence of
the enzyme was 72% homologous to that of a thermolabile
oligo-1,6-glucosidase (558 residues) from Bacillus cereus ATCC7064
(mesophile). B. cereus oligo-1,6-glucosidase contained 19 prolines.
Eighteen of these were conserved at the equivalent positions of B.
thermoglucosidasius oligo-1,6-glucosidase. This enzyme contained 14 extra
prolines besides the conservative prolines. The majority of extra prolines
was replaced by polar or charged residues (Glu, Thr, or Lys) in B. cereus
oligo-1,6-glucosidase. The extra prolines were responsible for the
difference in thermostability between these two enzymes. We suggested that
11 of the extra prolines in B. thermoglucosidasius oligo-1,6-glucosidase
occur in beta-turns or in coils within the loops binding adjacent secondary
structures.
Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6- glucosidase from Bacillus thermoglucosidasius KP1006
Department of Agricultural Chemistry, Kyoto Prefectural University, Japan.
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