1oa2
COMPARISON OF FAMILY 12 GLYCOSIDE HYDROLASES AND RECRUITED SUBSTITUTIONS IMPORTANT FOR THERMAL STABILITY
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OverviewOverview
As part of a program to discover improved glycoside hydrolase family 12, (GH 12) endoglucanases, we have studied the biochemical diversity of, several GH 12 homologs. The H. schweinitzii Cel12A enzyme differs from the, T. reesei Cel12A enzyme by only 14 amino acids (93% sequence identity), but is much less thermally stable. The bacterial Cel12A enzyme from S. sp., 11AG8 shares only 28% sequence identity to the T. reesei enzyme, and is, much more thermally stable. Each of the 14 sequence differences from H., schweinitzii Cel12A were introduced in T. reesei Cel12A to determine the, effect of these amino acid substitutions on enzyme stability. Several of, the T. reesei Cel12A variants were found to have increased stability, and, the differences in apparent midpoint of thermal denaturation ... [(full description)]
About this StructureAbout this Structure
1OA2 is a [Single protein] structure of sequence from [Trichoderma reesei] with NAG as [ligand]. Active as [[1]], with EC number [3.2.1.4]. Full crystallographic information is available from [OCA].
ReferenceReference
Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability., Sandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C, Protein Sci. 2003 Apr;12(4):848-60. PMID:12649442
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