A mutation study of catalytic residue Asp 52 in hen egg lysozyme.

A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Research Abstract Details 

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A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Abstract Text:

Y Hashimoto,K Yamada,H Motoshima,T Omura,H Yamada,T Yasukochi,T Miki,T Ueda,T Imoto,

We constructed a system for the expression and secretion of mature hen lysozyme by yeast using an intermediate "secretion-signal cassette" vector, pKP1700, containing the yeast invertase signal sequence and an expression vector, pAM82, for secretion and maturation of the enzyme. Using this system, mutants of hen lysozyme were produced and the catalytic mechanism in hen lysozyme was definitely confirmed. The hydrolytic activity of D52A as to substrate (NAG)6 at pH 5.0 was obviously decreased to one-four hundredth of that of the wild type. The acidic limb of the pH-activity profile observed for the wild-type was not observed for D52A, and the pKa of Glu 35 on the alkaline limb was seen for both enzymes. Moreover, no structural change was detected on X-ray analysis of D52A. Therefore, we confirmed that dissociated Asp 52 assists catalysis by producing an electrostatic field and by stabilizing the oxocarbonium ion intermediate in the dissociated form.

A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Publishing Authors By Initials

Y Hashimoto,K Yamada,H Motoshima,T Omura,H Yamada,T Yasukochi,T Miki,T Ueda,T Imoto,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: beta-fructofuranosidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: beta-fructofuranosidase research

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A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 119

Page Numbers: 145-50

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1996

A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Information

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LANGUAGE: eng

NlmUniqueID: 376600

A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Keywords Mesh Terms:

KEYWORDS: beta-Fructofuranosidase

MESH TERMS: genetics

Chemical & Substance for Abstract: A mutation study of catalytic residue Asp 52 in hen egg lysozyme. Information

Substance Name: beta-Fructofuranosidase

Registry Number: EC 3.2.1.26

Grant and Affiliation Information for A mutation study of catalytic residue Asp 52 in hen egg lysozyme.

AFFILIATION: Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka.

Country: JAPAN

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MEDLINETA: J Biochem

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