Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

Mamoru Nishimoto; Masafumi Hidaka; Masahiro Nakajima; Shinya Fushinobu; Motomitsu Kitaoka

doi:10.1016/j.molcatb.2011.09.004

Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

Mamoru Nishimoto, Masafumi Hidaka, Masahiro Nakajima, Shinya Fushinobu, Motomitsu Kitaoka

AGR - Life Sciences

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

Three amino acid residues of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (GalHexNAcP) were assigned as the determinants of substrate preference for galacto-N-biose (GNB) and lacto-N-biose I (LNB) based on the three-dimensional structure of the protein. Mutants of GalHexNAcP from Bifidobacterium longum, which acts similarly on both GNB and LNB, were constructed and characterized. V162T mutation led to an increase in the selectivity on GNB. P161S and S336A mutations independently enhanced the selectivity on LNB. The alignment of amino acid sequences suggests that the activities of most homologous sequences are predictable by comparing the corresponding three residues. .

Original language	English
Pages (from-to)	97-102
Number of pages	6
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	74
Issue number	1-2
DOIs	https://doi.org/10.1016/j.molcatb.2011.09.004
Publication status	Published - 2012 Jan 1

Keywords

1,3-β-Galactosyl-N-acetylhexosamine phosphorylase
Determinant residue of substrate preference
Galacto-N-biose
Glycoside hydrolase family 112
Lacto-N-biose I

ASJC Scopus subject areas

Catalysis
Bioengineering
Biochemistry
Process Chemistry and Technology

Access to Document

10.1016/j.molcatb.2011.09.004

Fingerprint Dive into the research topics of 'Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase'. Together they form a unique fingerprint.

Cite this

Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase. / Nishimoto, Mamoru; Hidaka, Masafumi; Nakajima, Masahiro; Fushinobu, Shinya; Kitaoka, Motomitsu.

In: Journal of Molecular Catalysis B: Enzymatic, Vol. 74, No. 1-2, 01.01.2012, p. 97-102.

Research output: Contribution to journal › Article › peer-review

@article{5c507e3b7b1a446282daf9b8f5227aca,

title = "Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase",

abstract = "Three amino acid residues of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (GalHexNAcP) were assigned as the determinants of substrate preference for galacto-N-biose (GNB) and lacto-N-biose I (LNB) based on the three-dimensional structure of the protein. Mutants of GalHexNAcP from Bifidobacterium longum, which acts similarly on both GNB and LNB, were constructed and characterized. V162T mutation led to an increase in the selectivity on GNB. P161S and S336A mutations independently enhanced the selectivity on LNB. The alignment of amino acid sequences suggests that the activities of most homologous sequences are predictable by comparing the corresponding three residues. .",

keywords = "1,3-β-Galactosyl-N-acetylhexosamine phosphorylase, Determinant residue of substrate preference, Galacto-N-biose, Glycoside hydrolase family 112, Lacto-N-biose I",

author = "Mamoru Nishimoto and Masafumi Hidaka and Masahiro Nakajima and Shinya Fushinobu and Motomitsu Kitaoka",

year = "2012",

month = jan,

day = "1",

doi = "10.1016/j.molcatb.2011.09.004",

language = "English",

volume = "74",

pages = "97--102",

journal = "Journal of Molecular Catalysis B: Enzymatic",

issn = "1381-1177",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Identification of amino acid residues that determine the substrate preference of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

AU - Nishimoto, Mamoru

AU - Hidaka, Masafumi

AU - Nakajima, Masahiro

AU - Fushinobu, Shinya

AU - Kitaoka, Motomitsu

PY - 2012/1/1

Y1 - 2012/1/1

N2 - Three amino acid residues of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (GalHexNAcP) were assigned as the determinants of substrate preference for galacto-N-biose (GNB) and lacto-N-biose I (LNB) based on the three-dimensional structure of the protein. Mutants of GalHexNAcP from Bifidobacterium longum, which acts similarly on both GNB and LNB, were constructed and characterized. V162T mutation led to an increase in the selectivity on GNB. P161S and S336A mutations independently enhanced the selectivity on LNB. The alignment of amino acid sequences suggests that the activities of most homologous sequences are predictable by comparing the corresponding three residues. .

AB - Three amino acid residues of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase (GalHexNAcP) were assigned as the determinants of substrate preference for galacto-N-biose (GNB) and lacto-N-biose I (LNB) based on the three-dimensional structure of the protein. Mutants of GalHexNAcP from Bifidobacterium longum, which acts similarly on both GNB and LNB, were constructed and characterized. V162T mutation led to an increase in the selectivity on GNB. P161S and S336A mutations independently enhanced the selectivity on LNB. The alignment of amino acid sequences suggests that the activities of most homologous sequences are predictable by comparing the corresponding three residues. .

KW - 1,3-β-Galactosyl-N-acetylhexosamine phosphorylase

KW - Determinant residue of substrate preference

KW - Galacto-N-biose

KW - Glycoside hydrolase family 112

KW - Lacto-N-biose I

UR - http://www.scopus.com/inward/record.url?scp=80054960221&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80054960221&partnerID=8YFLogxK

U2 - 10.1016/j.molcatb.2011.09.004

DO - 10.1016/j.molcatb.2011.09.004

M3 - Article

AN - SCOPUS:80054960221

VL - 74

SP - 97

EP - 102

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

SN - 1381-1177

IS - 1-2

ER -