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α-Amylases from Archaea: Sequences, Structures and Evolution

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Biotechnology of Extremophiles:

Part of the book series: Grand Challenges in Biology and Biotechnology ((GCBB,volume 1))

Abstract

α-Amylase (EC 3.2.1.1) catalyzes the hydrolysis of α-1,4-glucosidic linkages in starch and related α-glucans. Within the sequence-based classification of carbohydrate-active enzymes, the CAZy database, the specificity of α-amylase has been classified in glycoside hydrolase (GH) families GH13, GH57 and GH119. The polyspecific family GH13 with about 24,000 members is considered as the main α-amylase family forming the clan GH-H with families GH70 and GH77 (both without the α-amylase specificity). The family GH57, which is also a polyspecific one with, however, only about 1100 members, is known as the second α-amylase family related to the monospecific family GH119 (currently only 10 members). The α-amylases from the family GH13 employ a retaining reaction mechanism, share 7 conserved sequence regions (CSRs) and adopt a TIM-barrel domain with the GH13 catalytic machinery. Although the α-amylases from the family GH57 also use the retaining reaction mechanism, they exhibit their own 5 CSRs and have the catalytic machinery different from that present in the family GH13 within an incomplete TIM-barrel fold. In Archaea, α-amylases from families GH13 and GH57 have been found. The archaeal GH13 α-amylases form their subfamily GH13_7 that is remarkably closely related to the subfamily GH13_6 containing plant counterparts. There may also be another halophilic group of archaeal α-amylases in the family GH13 but currently without subfamily assignment. The archaeal GH57 α-amylases are most closely related to their α-amylase-like homologues, which are putative proteins with incomplete catalytic machinery originating mostly from Bacteria.

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Acknowledgement

Financial support from the Slovak Grant Agency VEGA (grant No. 2/0150/14) and the Slovak Research and Development Agency APVV (contract No. LPP-0417-09) is gratefully acknowledged.

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  1. Laboratory of Protein Evolution, Institute of Molecular Biology, Slovak Academy of Sciences, Dubravska cesta 2, SK-84551, Bratislava, Slovakia

    Štefan Janeček

  2. Faculty of Natural Sciences, Department of Biology, University of SS Cyril and Methodius, Nam. J. Herdu 2, SK-91701, Trnava, Slovakia

    Štefan Janeček

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  1. Federal University of Rio Grande do Sul, Porto Alegre, Rio Grande do Sul, Saint Barthélemy

    Pabulo H Rampelotto

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Janeček, Š. (2016). α-Amylases from Archaea: Sequences, Structures and Evolution. In: Rampelotto, P. (eds) Biotechnology of Extremophiles:. Grand Challenges in Biology and Biotechnology, vol 1. Springer, Cham. https://doi.org/10.1007/978-3-319-13521-2_17

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