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Streptococcus Agalactiae Amylomaltase Offers Insight Into the Transglycosylation Mechanism and the Molecular Basis of Thermostability Among Amylomaltases by Tumhom, Suthipapun (author);Nimpiboon, Pitchanan (author);Wangkanont, Kittikhun (author);Pongsawasdi, Piamsook (author) is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Amylomaltase (AM) catalyzes transglycosylation of starch to form linear or cyclic oligosaccharides with potential applications in biotechnology and industry. In the present work, a novel AM from the mesophilic bacterium Streptococcus agalactiae (SaAM), with 18–49% sequence identity to previously reported AMs, was characterized. Cyclization and disproportionation activities were observed with the optimum temperature of 30 °C and 40 °C, respectively. Structural determination of SaAM, the first crystal structure of small AMs from the mesophiles, revealed a glycosyl-enzyme intermediate derived from acarbose and a second acarbose molecule attacking the intermediate. This pre-transglycosylation conformation has never been before observed in AMs. Structural analysis suggests that thermostability in AMs might be mainly caused by an increase in salt bridges since SaAM has a lower number of salt bridges compared with AMs from the thermophiles. Increase in thermostability by mutation was performed. C446 was substituted with A/S/P. C446A showed higher activities and higher k~cat~/K~m~ values for starch in comparison to the WT enzyme. C446S exhibited a 5 °C increase in optimum tempe

Who reads Streptococcus Agalactiae Amylomaltase Offers Insight Into the Transglycosylation Mechanism and the Molecular Basis of Thermostability Among Amylomaltases?

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Author
Tumhom, Suthipapun (author);Nimpiboon, Pitchanan (author);Wangkanont, Kittikhun (author);Pongsawasdi, Piamsook (author)
Publisher
Springer Science and Business Media LLC
Published
2021
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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