Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)

Judit Remenyik; Chandran Ragunath; Narayanan Ramasubbu; Gyöngyi Gyémánt; András Lipták; Lili Kandra

doi:10.1021/ol035999k

Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)

Judit Remenyik, Chandran Ragunath, Narayanan Ramasubbu, Gyöngyi Gyémánt, András Lipták, Lili Kandra

School of Dental Medicine, Oral Biology

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

14 Scopus citations

Abstract

(Equation Presented) Synthesis of 4-nitrophenyl 1-thio-β-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary α-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. ¹H and ¹³C NMR studies revealed that the mutated enzyme preserved the stereo- and regioselectivity. The glycosylation took place at position 4 of the glycosyl acceptor, forming the α(1-4)glycosidic bond, exclusively.

Original language	English (US)
Pages (from-to)	4895-4898
Number of pages	4
Journal	Organic letters
Volume	5
Issue number	25
DOIs	https://doi.org/10.1021/ol035999k
State	Published - Dec 11 2003

All Science Journal Classification (ASJC) codes

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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title = "Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)",

abstract = "(Equation Presented) Synthesis of 4-nitrophenyl 1-thio-β-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary α-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. 1H and 13C NMR studies revealed that the mutated enzyme preserved the stereo- and regioselectivity. The glycosylation took place at position 4 of the glycosyl acceptor, forming the α(1-4)glycosidic bond, exclusively.",

author = "Judit Remenyik and Chandran Ragunath and Narayanan Ramasubbu and Gy{\"o}ngyi Gy{\'e}m{\'a}nt and Andr{\'a}s Lipt{\'a}k and Lili Kandra",

year = "2003",

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day = "11",

doi = "10.1021/ol035999k",

language = "English (US)",

volume = "5",

pages = "4895--4898",

journal = "Organic Letters",

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TY - JOUR

T1 - Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)

AU - Remenyik, Judit

AU - Ragunath, Chandran

AU - Ramasubbu, Narayanan

AU - Gyémánt, Gyöngyi

AU - Lipták, András

AU - Kandra, Lili

PY - 2003/12/11

Y1 - 2003/12/11

N2 - (Equation Presented) Synthesis of 4-nitrophenyl 1-thio-β-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary α-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. 1H and 13C NMR studies revealed that the mutated enzyme preserved the stereo- and regioselectivity. The glycosylation took place at position 4 of the glycosyl acceptor, forming the α(1-4)glycosidic bond, exclusively.

AB - (Equation Presented) Synthesis of 4-nitrophenyl 1-thio-β-D-maltoside, maltotrioside, and maltotetraoside in yields up to 60% has been achieved by a Tyr151Met (Y151M) mutant of human salivary α-amylase. Y151M is capable of transferring maltose and maltotriose residues from a maltotetraose donor onto different p-nitrophenyl glycosides. 1H and 13C NMR studies revealed that the mutated enzyme preserved the stereo- and regioselectivity. The glycosylation took place at position 4 of the glycosyl acceptor, forming the α(1-4)glycosidic bond, exclusively.

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JO - Organic Letters

JF - Organic Letters

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ER -

Introducing Transglycosylation Activity into Human Salivary α-Amylase (HSA)

Abstract

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