Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases

Sophie Bozonnet; Birgit Christine Bønsager; B. Kramhoft; H. Mori; Maher Abou Hachem; Martin Willemoes; M.T. Jensen; Kenji Fukuda; P.K. Nielsen; N. Juge; N. Aghajari; S. Tranier; X. Robert; R. Haser; Birte Svensson

Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases

Sophie Bozonnet, Birgit Christine Bønsager, B. Kramhoft, H. Mori, Maher Abou Hachem, Martin Willemoes, M.T. Jensen, Kenji Fukuda, P.K. Nielsen, N. Juge, N. Aghajari, S. Tranier, X. Robert, R. Haser, Birte Svensson

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

This review on barley alpha-amylases 1 (AMY1) and 2 (AMY2) addresses rational mutations at distal subsites to the catalytic site, polysaccharide hydrolysis, and interactions with proteinaceous inhibitors. Subsite mapping of barley alpha-amylases revealed 6 glycone and 4 aglycone substrate subsites. Moreover, two maltooligosaccharide surface binding sites have been identified. Engineering of outer subsites -6 and +4 alters action patterns and relative specificities. Thus, compared to wild-type, Y105A AMY1 (subsite -6) shows 140%, 15%, and

Original language	English
Journal	Biologia
Volume	60
Pages (from-to)	27-36
ISSN	0006-3088
Publication status	Published - 2005

Keywords

isozyme chimeras
amylopectin
proteinaceous inhibitors
degree of multiple attack
barley alpha-amylase
secondary binding sites
subsite mutants

OpenUrl availability

Full text

Cite this

@article{dc35f2433dd94b78846565cdc4c0c729,

title = "Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases",

abstract = "This review on barley alpha-amylases 1 (AMY1) and 2 (AMY2) addresses rational mutations at distal subsites to the catalytic site, polysaccharide hydrolysis, and interactions with proteinaceous inhibitors. Subsite mapping of barley alpha-amylases revealed 6 glycone and 4 aglycone substrate subsites. Moreover, two maltooligosaccharide surface binding sites have been identified. Engineering of outer subsites -6 and +4 alters action patterns and relative specificities. Thus, compared to wild-type, Y105A AMY1 (subsite -6) shows 140%, 15%, and ",

keywords = "isozyme chimeras, amylopectin, proteinaceous inhibitors, degree of multiple attack, barley alpha-amylase, secondary binding sites, subsite mutants",

author = "Sophie Bozonnet and B{\o}nsager, {Birgit Christine} and B. Kramhoft and H. Mori and {Abou Hachem}, Maher and Martin Willemoes and M.T. Jensen and Kenji Fukuda and P.K. Nielsen and N. Juge and N. Aghajari and S. Tranier and X. Robert and R. Haser and Birte Svensson",

year = "2005",

language = "English",

volume = "60",

pages = "27--36",

journal = "Biologia",

issn = "0006-3088",

publisher = "Walterde Gruyter GmbH",

}

TY - JOUR

T1 - Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases

AU - Bozonnet, Sophie

AU - Bønsager, Birgit Christine

AU - Kramhoft, B.

AU - Mori, H.

AU - Abou Hachem, Maher

AU - Willemoes, Martin

AU - Jensen, M.T.

AU - Fukuda, Kenji

AU - Nielsen, P.K.

AU - Juge, N.

AU - Aghajari, N.

AU - Tranier, S.

AU - Robert, X.

AU - Haser, R.

AU - Svensson, Birte

PY - 2005

Y1 - 2005

N2 - This review on barley alpha-amylases 1 (AMY1) and 2 (AMY2) addresses rational mutations at distal subsites to the catalytic site, polysaccharide hydrolysis, and interactions with proteinaceous inhibitors. Subsite mapping of barley alpha-amylases revealed 6 glycone and 4 aglycone substrate subsites. Moreover, two maltooligosaccharide surface binding sites have been identified. Engineering of outer subsites -6 and +4 alters action patterns and relative specificities. Thus, compared to wild-type, Y105A AMY1 (subsite -6) shows 140%, 15%, and

AB - This review on barley alpha-amylases 1 (AMY1) and 2 (AMY2) addresses rational mutations at distal subsites to the catalytic site, polysaccharide hydrolysis, and interactions with proteinaceous inhibitors. Subsite mapping of barley alpha-amylases revealed 6 glycone and 4 aglycone substrate subsites. Moreover, two maltooligosaccharide surface binding sites have been identified. Engineering of outer subsites -6 and +4 alters action patterns and relative specificities. Thus, compared to wild-type, Y105A AMY1 (subsite -6) shows 140%, 15%, and

KW - isozyme chimeras

KW - amylopectin

KW - proteinaceous inhibitors

KW - degree of multiple attack

KW - barley alpha-amylase

KW - secondary binding sites

KW - subsite mutants

M3 - Journal article

SN - 0006-3088

VL - 60

SP - 27

EP - 36

JO - Biologia

JF - Biologia

ER -

Binding of carbohydrates and protein inhibitors to the surface of alpha-amylases

Abstract

Keywords

OpenUrl availability

Fingerprint

Cite this