Structural highlights
Publication Abstract from PubMed
A novel alpha-amylase (McAmyA) from the thermophilic fungus, Malbranchea cinnamomea was purified, characterized and crystallized in the present study. McAmyA was purified to apparent homogeneity with a molecular mass of 60.3 kDa on SDS-PAGE. The enzyme exhibited maximal activity at pH 6.5 and was stable within pH 5.0-10.0. It was most active at 65 degrees C and was stable up to 50 degrees C. McAmyA was capable of hydrolyzing amylose, starch, amylopectin, pullulan, cyclodextrins and maltooligosaccharides. The full-length cDNA of an alpha-amylase gene (McAmyA) from the strain was cloned. McAmyA consisted of a 1,476-bp open reading frame encoding 492 amino acids. It displayed the highest amino acid sequence homology (less than 60 %) with the reported alpha-amylases. The crystal structure of McAmyA was solved at a resolution of 2.25 A (PDB code 3VM7). The overall structure of McAmyA reveals three domains with ten alpha helices and 14 beta strands, and the putative catalytic residues are positioned at domain A with somewhat different secondary structural circumstances compared with typical alpha-amylases.
A novel multifunctional alpha-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.,Han P, Zhou P, Hu S, Yang S, Yan Q, Jiang Z Appl Biochem Biotechnol. 2013 May;170(2):420-35. doi: 10.1007/s12010-013-0198-y. , Epub 2013 Mar 29. PMID:23536251[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Han P, Zhou P, Hu S, Yang S, Yan Q, Jiang Z. A novel multifunctional alpha-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure. Appl Biochem Biotechnol. 2013 May;170(2):420-35. doi: 10.1007/s12010-013-0198-y. , Epub 2013 Mar 29. PMID:23536251 doi:10.1007/s12010-013-0198-y
