Solution structure and activity of mouse lysozyme M

T. Obita, Tadashi Ueda, T. Imoto

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR spectroscopy. We found that mouse lysozyme M had four α-helices, two 310 helices, and a double- and a triple-stranded anti-parallel β-sheet, and its structure was very similar to that of hen lysozyme in solution and in the crystalline state. The pH activity profile of p-nitrophenyl penta N-acetyl-β-D-chitopentaoside hydrolysis by mouse lysozyme M was similar to that of hen lysozyme, but the hydrolytic activity of mouse lysozyme M was lower. From analyses of binding affinities of lysozymes to a substrate analogue and internal motions of lysozymes, we suggest that the lower activity of mouse lysozyme M was due to the larger dissociation constant of its enzyme-substrate complex and the restricted internal backbone motions in the molecule.

Original languageEnglish
Pages (from-to)176-184
Number of pages9
JournalCellular and Molecular Life Sciences
Volume60
Issue number1
DOIs
Publication statusPublished - Jan 1 2003

Fingerprint

Muramidase
Biomolecular Nuclear Magnetic Resonance
Rubiaceae
Glycoside Hydrolases
Substrates
Nuclear magnetic resonance spectroscopy
Hydrolysis
Magnetic Resonance Spectroscopy
mouse lysozyme M
Crystalline materials
Amino Acids
Molecules
Enzymes

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

Solution structure and activity of mouse lysozyme M. / Obita, T.; Ueda, Tadashi; Imoto, T.

In: Cellular and Molecular Life Sciences, Vol. 60, No. 1, 01.01.2003, p. 176-184.

Research output: Contribution to journalArticle

@article{003f894d4a0f41388ea5169d8a200b12,
title = "Solution structure and activity of mouse lysozyme M",
abstract = "The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR spectroscopy. We found that mouse lysozyme M had four α-helices, two 310 helices, and a double- and a triple-stranded anti-parallel β-sheet, and its structure was very similar to that of hen lysozyme in solution and in the crystalline state. The pH activity profile of p-nitrophenyl penta N-acetyl-β-D-chitopentaoside hydrolysis by mouse lysozyme M was similar to that of hen lysozyme, but the hydrolytic activity of mouse lysozyme M was lower. From analyses of binding affinities of lysozymes to a substrate analogue and internal motions of lysozymes, we suggest that the lower activity of mouse lysozyme M was due to the larger dissociation constant of its enzyme-substrate complex and the restricted internal backbone motions in the molecule.",
author = "T. Obita and Tadashi Ueda and T. Imoto",
year = "2003",
month = "1",
day = "1",
doi = "10.1007/s000180300012",
language = "English",
volume = "60",
pages = "176--184",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Birkhauser Verlag Basel",
number = "1",

}

TY - JOUR

T1 - Solution structure and activity of mouse lysozyme M

AU - Obita, T.

AU - Ueda, Tadashi

AU - Imoto, T.

PY - 2003/1/1

Y1 - 2003/1/1

N2 - The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR spectroscopy. We found that mouse lysozyme M had four α-helices, two 310 helices, and a double- and a triple-stranded anti-parallel β-sheet, and its structure was very similar to that of hen lysozyme in solution and in the crystalline state. The pH activity profile of p-nitrophenyl penta N-acetyl-β-D-chitopentaoside hydrolysis by mouse lysozyme M was similar to that of hen lysozyme, but the hydrolytic activity of mouse lysozyme M was lower. From analyses of binding affinities of lysozymes to a substrate analogue and internal motions of lysozymes, we suggest that the lower activity of mouse lysozyme M was due to the larger dissociation constant of its enzyme-substrate complex and the restricted internal backbone motions in the molecule.

AB - The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR spectroscopy. We found that mouse lysozyme M had four α-helices, two 310 helices, and a double- and a triple-stranded anti-parallel β-sheet, and its structure was very similar to that of hen lysozyme in solution and in the crystalline state. The pH activity profile of p-nitrophenyl penta N-acetyl-β-D-chitopentaoside hydrolysis by mouse lysozyme M was similar to that of hen lysozyme, but the hydrolytic activity of mouse lysozyme M was lower. From analyses of binding affinities of lysozymes to a substrate analogue and internal motions of lysozymes, we suggest that the lower activity of mouse lysozyme M was due to the larger dissociation constant of its enzyme-substrate complex and the restricted internal backbone motions in the molecule.

UR - http://www.scopus.com/inward/record.url?scp=0037278025&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037278025&partnerID=8YFLogxK

U2 - 10.1007/s000180300012

DO - 10.1007/s000180300012

M3 - Article

C2 - 12613666

AN - SCOPUS:0037278025

VL - 60

SP - 176

EP - 184

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 1

ER -