Publication

Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity

Zhang, X., Leemhuis, H., Janeček, Š., Martinovičová, M., Pijning, T. & van der Maarel, M. J. E. C., Aug-2019, In : Applied Microbiology and Biotechnology. 103, p. 6141–6151

Research output: Contribution to journalArticleAcademicpeer-review

APA

Zhang, X., Leemhuis, H., Janeček, Š., Martinovičová, M., Pijning, T., & van der Maarel, M. J. E. C. (2019). Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. Applied Microbiology and Biotechnology, 103, 6141–6151. https://doi.org/10.1007/s00253-019-09938-1

Author

Zhang, Xuewen ; Leemhuis, Hans ; Janeček, Štefan ; Martinovičová, Mária ; Pijning, Tjaard ; van der Maarel, Marc J. E. C. / Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. In: Applied Microbiology and Biotechnology. 2019 ; Vol. 103. pp. 6141–6151.

Harvard

Zhang, X, Leemhuis, H, Janeček, Š, Martinovičová, M, Pijning, T & van der Maarel, MJEC 2019, 'Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity' Applied Microbiology and Biotechnology, vol. 103, pp. 6141–6151. https://doi.org/10.1007/s00253-019-09938-1

Standard

Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. / Zhang, Xuewen; Leemhuis, Hans; Janeček, Štefan; Martinovičová, Mária; Pijning, Tjaard; van der Maarel, Marc J. E. C.

In: Applied Microbiology and Biotechnology, Vol. 103, 08.2019, p. 6141–6151.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Zhang X, Leemhuis H, Janeček Š, Martinovičová M, Pijning T, van der Maarel MJEC. Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity. Applied Microbiology and Biotechnology. 2019 Aug;103:6141–6151. https://doi.org/10.1007/s00253-019-09938-1


BibTeX

@article{426394605ebc499db093db6f8e320dec,
title = "Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity",
abstract = "AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular α-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism. However, the α-amylase specificity of AmyC is questionable as extensive phylogenetic analysis of GH57 and tertiary structural comparison suggest that AmyC could actually be a glycogen-branching enzyme (GBE), a key enzyme in the biosynthesis of glycogen. This communication presents phylogenetic and biochemical evidence that AmyC is a GBE with a relatively high hydrolytic (α-amylase) activity (up to 30{\%} of the total activity), creating a branched α-glucan with 8.5{\%} α-1,6-glycosidic bonds. The high hydrolytic activity is explained by the fact that AmyC has a considerably shorter catalytic loop (residues 213-220) not reaching the acceptor side. Secondly, in AmyC, the tryptophan residue (W 246) near the active site has its side chain buried in the protein interior, while the side chain is at the surface in Tk1436 and Tt1467 GBEs. The putative GBEs from three other Thermotogaceae, with very high sequence similarities to AmyC, were found to have the same structural elements as AmyC, suggesting that GH57 GBEs with relatively high hydrolytic activity may be widespread in nature.",
author = "Xuewen Zhang and Hans Leemhuis and Štefan Janeček and M{\'a}ria Martinovičov{\'a} and Tjaard Pijning and {van der Maarel}, {Marc J. E. C.}",
year = "2019",
month = "8",
doi = "10.1007/s00253-019-09938-1",
language = "English",
volume = "103",
pages = "6141–6151",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "SPRINGER",

}

RIS

TY - JOUR

T1 - Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity

AU - Zhang, Xuewen

AU - Leemhuis, Hans

AU - Janeček, Štefan

AU - Martinovičová, Mária

AU - Pijning, Tjaard

AU - van der Maarel, Marc J. E. C.

PY - 2019/8

Y1 - 2019/8

N2 - AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular α-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism. However, the α-amylase specificity of AmyC is questionable as extensive phylogenetic analysis of GH57 and tertiary structural comparison suggest that AmyC could actually be a glycogen-branching enzyme (GBE), a key enzyme in the biosynthesis of glycogen. This communication presents phylogenetic and biochemical evidence that AmyC is a GBE with a relatively high hydrolytic (α-amylase) activity (up to 30% of the total activity), creating a branched α-glucan with 8.5% α-1,6-glycosidic bonds. The high hydrolytic activity is explained by the fact that AmyC has a considerably shorter catalytic loop (residues 213-220) not reaching the acceptor side. Secondly, in AmyC, the tryptophan residue (W 246) near the active site has its side chain buried in the protein interior, while the side chain is at the surface in Tk1436 and Tt1467 GBEs. The putative GBEs from three other Thermotogaceae, with very high sequence similarities to AmyC, were found to have the same structural elements as AmyC, suggesting that GH57 GBEs with relatively high hydrolytic activity may be widespread in nature.

AB - AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular α-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism. However, the α-amylase specificity of AmyC is questionable as extensive phylogenetic analysis of GH57 and tertiary structural comparison suggest that AmyC could actually be a glycogen-branching enzyme (GBE), a key enzyme in the biosynthesis of glycogen. This communication presents phylogenetic and biochemical evidence that AmyC is a GBE with a relatively high hydrolytic (α-amylase) activity (up to 30% of the total activity), creating a branched α-glucan with 8.5% α-1,6-glycosidic bonds. The high hydrolytic activity is explained by the fact that AmyC has a considerably shorter catalytic loop (residues 213-220) not reaching the acceptor side. Secondly, in AmyC, the tryptophan residue (W 246) near the active site has its side chain buried in the protein interior, while the side chain is at the surface in Tk1436 and Tt1467 GBEs. The putative GBEs from three other Thermotogaceae, with very high sequence similarities to AmyC, were found to have the same structural elements as AmyC, suggesting that GH57 GBEs with relatively high hydrolytic activity may be widespread in nature.

U2 - 10.1007/s00253-019-09938-1

DO - 10.1007/s00253-019-09938-1

M3 - Article

VL - 103

SP - 6141

EP - 6151

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

ER -

ID: 85447434