Michiro Muraki

ORCID: 0000-0003-4953-8007
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Enzyme Structure and Function
  • Protein Structure and Dynamics
  • Cell death mechanisms and regulation
  • Toxin Mechanisms and Immunotoxins
  • Carbohydrate Chemistry and Synthesis
  • Enzyme Production and Characterization
  • Transgenic Plants and Applications
  • Biochemical and Structural Characterization
  • Biochemical and Molecular Research
  • RNA Interference and Gene Delivery
  • Cancer, Hypoxia, and Metabolism
  • Chemical Synthesis and Analysis
  • Phagocytosis and Immune Regulation
  • Peptidase Inhibition and Analysis
  • Child and Adolescent Psychosocial and Emotional Development
  • Maternal Mental Health During Pregnancy and Postpartum
  • Infant Development and Preterm Care
  • Porphyrin Metabolism and Disorders
  • SARS-CoV-2 and COVID-19 Research
  • Galectins and Cancer Biology
  • interferon and immune responses
  • Pharmacological Effects of Natural Compounds
  • Medicinal plant effects and applications
  • Cancer Research and Treatments

Hitachi (Japan)
2022

National Institute of Advanced Industrial Science and Technology
2006-2020

Hamamatsu University
2019

University of Tsukuba
1995

Nitto Chemical Industry (Japan)
1985-1992

Public Works Research Institute
1992

National Chemical Laboratory
1985-1989

Osaka City University
1982

Abstract The specific interaction of a variety modified hevein domains to chitooligosaccharides has been studied by NMR spectroscopy in order assess the importance aromatic–carbohydrate interactions for molecular recognition neutral sugars. These mutant AcAMP2‐like peptides, which have 4‐fluoro‐phenylalanine, tryptophan, or 2‐naphthylalanine at key interacting positions, prepared solid‐phase synthesis. Their three‐dimensional structures, when bound chitin‐derived trisaccharide, deduced...

10.1002/chem.200500367 article EN Chemistry - A European Journal 2005-10-12

The three-dimensional structure of human alpha-lactalbumin for two crystal forms has been determined by x-ray analysis. One (the form LT) was obtained at pH 4.2 and room temperature, while the other HT) grown 6.5 37 degrees C. backbone Lys1-Ile95 residues is almost conserved between structures as indicated root mean square difference 0.30 A superposition equivalent C alpha atoms. calcium ion surrounded seven oxygen atoms three carboxyl groups, carbonyl water molecules, which a distorted...

10.1016/s0021-9258(18)45959-5 article EN cc-by Journal of Biological Chemistry 1992-01-01

10.1016/s0304-4165(01)00231-8 article EN Biochimica et Biophysica Acta (BBA) - General Subjects 2002-01-01

To get high level secretion of human lysozyme in Pichia pastoris, the following three signal sequences and one prepro sequence were evaluated: chicken peptide, leucine-rich artificial Saccharomyces invertase alpha factor (MF-α Prepro). Transformants harboring a gene with MF-α Prepro secreted 20-fold more than those any other sequences. Three mutant leader derived from constructed to discover function pro region. The was dramatically decreased by eliminating region Prepro. In contrast, EAEAEA...

10.1271/bbb.63.1977 article EN Bioscience Biotechnology and Biochemistry 1999-01-01

The surface positive charges of human lysozyme were either increased or decreased to alter the electrostatic interaction between enzyme and substrate in lytic action using site-directed mutagenesis. amino acid substitutions accompanying addition removal two units charge have shifted optimal ionic strength (NaCl concentration 10 mM Mes buffer, pH 6.2) for lysis Micrococcus lysodeikticus cell from 0.04 M 0.1 0.02 respectively. In change strength-activity profile, pH-activity profile effect a...

10.1093/protein/2.1.49 article EN Protein Engineering Design and Selection 1988-01-01

In order to reveal the origin of carbohydrate recognition specificity human lysozyme by clarifying difference in binding mode ligands active site, inactivation 2',3'-epoxypropyl β-glycoside derivatives disaccharides, N,N'-diacetylchitobiose [GlcNAc-β-(1→4)-GlcNAc] and N-acetyllactosamine [Gal-β-(1→4)-GlcNAc], was investigated three-dimensional structures affinity-labeled enzymes were determined X-ray crystallography at 1.7 Å resolution. Under conditions comprising 2.0 × 10-3 M labeling...

10.1021/bi9613180 article EN Biochemistry 1996-01-01

Chemically prepared hevein domains (HDs), N-terminal domain of an antifungal protein from Nicotiana tabacum (CBP20-N) and antimicrobial peptide Amaranthus caudatus (Ac-AMP2), were examined for their affinity chitin, a β-1,4-linked polymer N-acetylglucosamine. An intact binding domain, CBP20-N, showed higher than C-terminal truncated Ac-AMP2. The formation pyroglutamate residue Gln CBP20-N increased the affinity. single replacement any aromatic Ac-AMP2 with Ala resulted in significant...

10.1093/protein/13.6.385 article EN Protein Engineering Design and Selection 2000-06-01

The synergism between apolar and polar interactions in the carbohydrate recognition by human lysozyme (HL) was probed site-directed mutagenesis affinity labeling. three-dimensional structures of Tyr63-->Leu mutant HL labeled with 2',3'-epoxypropyl beta-glycoside N,N'-diacetylchitobiose (L63-HL/NAG-NAG-EPO complex) Asp102-->Glu N-acetyllactosamine were revealed X-ray diffraction at 2.23 1.96 A resolution, respectively. Compared to wild-type 2', 3'-epoxypropyl N,N'-diacetylchitobiose,...

10.1021/bi991402q article EN Biochemistry 1999-12-17

Crystal structures of turkey egg lysozyme (TEL) and human (HL) were refined by full-matrix least-squares method using anisotropic temperature factors. The refinement converged at the conventional R-values 0.104 0.115 for reflections with Fo > 0 to resolution 1.12 Å 1.15 Å, respectively. estimated r.m.s. coordinate errors protein atoms 0.031 0.034 (HL). introduction factors markedly reduced R-value but did not significantly affect main chain coordinates. degree anisotropy atomic thermal...

10.1002/(sici)1097-0134(19980215)30:3<232::aid-prot3>3.0.co;2-m article EN Proteins Structure Function and Bioinformatics 1998-02-15

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDissection of the functional role structural elements tyrosine-63 in catalytic action human lysozymeMichiro Muraki, Kazuaki Harata, and Yoshifumi JigamiCite this: Biochemistry 1992, 31, 38, 9212–9219Publication Date (Print):September 1, 1992Publication History Published online1 May 2002Published inissue 1 September 1992https://doi.org/10.1021/bi00153a014RIGHTS & PERMISSIONSArticle Views118Altmetric-Citations23LEARN ABOUT THESE METRICSArticle Views...

10.1021/bi00153a014 article EN Biochemistry 1992-09-01

A 418 base pair DNA duplex consisting of a gene for human lysozyme with synthetic ribosome binding site E. coli was assembled by stepwise ligation 56 chemically synthesized oligodeoxyribonucleotides. The expressed under the control lambda pRpL promoter and tfie product accumulated as several percent total cellular proteins in coli. existed insoluble biologically inactive aggregates cells, but biological activity regenerated solubilization renaturation aggregated protein. results N-terminal...

10.1080/00021369.1986.10867445 article EN Agricultural and Biological Chemistry 1986-03-01

Genes encoding pre‐protein and prepro‐protein of wheat germ agglutinin isolectin 2 (WGA2) were chemically synthesized expressed in the yeast Saccharomyces cerevisiae under control ENO1 promoter. Yeast harboring either a pre‐WGA2 or prepro‐WGA2 gene expression plasmid secreted mature form WGA2 into culture medium. The amount by strain KS58‐2Ddel, which has ssll mutation causing supersecretion human lysozyme [Suzuki, K., Ichikawa, K. &amp; Jigami, Y. (1989) Mol. Gen. Genet. 219 , 58–64], was...

10.1111/j.1432-1033.1992.tb17504.x article EN European Journal of Biochemistry 1992-12-01

Ultica dioica agglutinin, a plant lectin from the stinging nettle, consists of total seven individual isolectins. One these structures, isolectin I, was determined at 1.9 A resolution by X-ray method. The crystals belong to space group P2(1) and asymmetric unit contains two molecules related local twofold symmetry. molecule hevein-like chitin-binding domains lacking distinct secondary structure, but four disulfide bonds in each domain maintain tertiary structure. backbone structure...

10.1107/s090744490101232x article EN Acta Crystallographica Section D Biological Crystallography 2001-10-25

The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. crystal structure determined by molecular replacement refined to an R value of 0.182 using 10–1.77 Å data. molecule occupies the subsites A, B C. At C, sugar residues are bound in a similar manner that found hen-egg (HEL) complex. In contrast, GlcNac residue subsite A is exposed bulk solvent has no contact protein because active Asp101 HEL replaced...

10.1107/s0907444997005362 article EN Acta Crystallographica Section D Biological Crystallography 1997-11-01
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