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Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfacesActive and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenaseThe crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductaseHeterogeneous nucleation of protein crystals on fluorinated layered silicateCloning, nucleotide sequencing, and expression in Escherichia coli of the gene for formate dehydrogenase of Paracoccus sp. 12-A, a formate-assimilating bacterium.D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum.Structural organization of the pigment cell-specific gene located at the brown locus in mouse. Its promoter activity and alternatively spliced transcript.Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1.Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli.Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli.1,2-β-Oligoglucan phosphorylase from Listeria innocuaFunctional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocuaMechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentansSome Lactobacillus L-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetateTwo forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071.Chitin-deacetylase activity induces appressorium differentiation in the rice blast fungus Magnaporthe oryzae.Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family.Crystallization and preliminary X-ray diffraction analysis of Lin1840, a putative β-glucosidase from Listeria innocua.Diverse allosteric and catalytic functions of tetrameric d-lactate dehydrogenases from three Gram-negative bacteria.The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenaseHeat-stable extracellular proteolytic enzyme produced by Thermus caldophilus strain GK24, an extremely thermophilic bacterium.L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence.Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis--enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli.The Simple and Unique Allosteric Machinery of Thermus caldophilus Lactate Dehydrogenase : Structure-Function Relationship in Bacterial Allosteric LDHs.An absolute requirement of fructose 1,6-bisphosphate for the Lactobacillus casei L-lactate dehydrogenase activity induced by a single amino acid substitution.Recognition site for the side chain of 2-ketoacid substrate in d-lactate dehydrogenase.Function and structure relationships of a β-1,2-glucooligosaccharide-degrading β-glucosidase.The ternary complex structure of d-mandelate dehydrogenase with NADH and anilino(oxo)acetate.Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.Structural and thermodynamic insights into β-1,2-glucooligosaccharide capture by a solute-binding protein in Listeria innocua.Transcriptional control of rat heme oxygenase by heat shock.A molecular design that stabilizes active state in bacterial allosteric L-lactate dehydrogenasesStructural Basis of Sequential Allosteric Transitions in Tetrameric d-Lactate Dehydrogenases from Three Gram-Negative BacteriaCharacterization and Structural Analysis of a Novel exo-Type Enzyme Acting on β-1,2-Glucooligosaccharides from Parabacteroides distasonisThe active site of carboxypeptidase Taq possesses the active-site motif His-Glu-X-X-His of zinc-dependent endopeptidases and aminopeptidasesRole of histidine 188 in fructose 1,6-bisphosphate- and divalent cation-regulated L-lactate dehydrogenase of Lactobacillus caseiInvolvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysisA highly specific glyoxylate reductase derived from a formate dehydrogenaseSynthesis of three deoxy-sophorose derivatives for evaluating the requirement of hydroxy groups at position 3 and/or 3' of sophorose by 1,2-β-oligoglucan phosphorylases
P50
Q27637481-A03AE67F-2A8A-4F4D-9BE6-34028FB5AF13Q27657593-15535564-A1D6-4E11-9391-373A6D867218Q27685393-26ACCF14-1B27-4C76-87F2-274EAA739C7AQ28479484-AD60490B-DC4A-406A-9C6E-2DEE8B1C7ABDQ30708148-DEA525F8-77CA-4EFA-880B-DC55ADD87A9DQ31152300-74071CEA-549B-4F38-9205-6C955898F563Q33393175-D0A60D58-60E6-4751-BB8B-628825B8C9BEQ34247441-88B26C9D-A848-4095-BB71-F9DE96CB909DQ34311821-0FE15A5A-9BFD-4ECC-B4E2-3D92128DB5B0Q35119621-A22E3041-0502-49B9-8D69-2586EFE6F470Q35125354-22BEB505-9C4D-4D29-B667-4E7748ADE3D8Q35926200-7C570A0E-5E8C-4811-B2A3-CA01D270DBDDQ38289043-A627141F-D49F-4C2F-BA80-09B5046A901EQ39501860-267BE2EF-78F9-4F9A-9014-DB084523F299Q39649721-DC07BFCD-5DAE-4A92-9A2F-5F26A8419841Q40075524-A7DC8DE2-047A-4182-8DC4-9DE2E1170905Q40304455-DD756996-AD3E-4EA5-987E-201E8641ABB7Q41995702-FF6FD61E-64B5-498E-B35C-1E0BC30ADFCDQ42073648-5D9B0C1F-6623-4833-A28E-9FAFF8F8EF32Q42549596-C250356A-D1C1-4653-A02E-B014F4E76382Q43021025-124AD0CE-7AE2-4846-B9E6-185B86C86899Q43021197-9E9CEE8B-65FD-4044-A869-FB369B1599F8Q43021578-0AD662AE-71FA-482B-8CBF-818D7009A2E4Q43024908-A4138024-A150-4D7B-9631-32ECEC6E978FQ43028979-105E25F2-764C-497F-8707-B56967E03957Q43884460-14E9487E-FF77-4B8D-AF84-76D87EAC377DQ46905167-2834BACF-0E8F-4F10-A036-ED87503BA277Q47409613-03C93B6C-36BB-4A21-8719-A73D4C6E0774Q51091262-E539DB5D-7145-4962-827A-6AD355F9266BQ54207610-8609C6BE-F500-4171-BC34-250A77E63E70Q54231312-E1689699-FDFA-4525-9406-9255895F3D8FQ54761182-73873F5C-DB7B-41A1-B08F-FB08AFA6A1EDQ56895998-6CDC9F96-F64F-4FA9-A761-7EC432AE8613Q57983495-59162A19-9D3E-4DC3-AD18-B59807520CE0Q57983496-D63EE3C1-D0B5-4B14-B351-F181993BDF25Q71665426-F9B34782-39F8-4720-A3D5-288C1C1AD48CQ72276430-B7DA5118-0935-413C-801B-40AB37B14EFBQ73942900-CD233311-522F-455D-B700-76599FB5A310Q79827265-6A356067-463E-44DD-BF0D-4DCBC354334EQ91019732-9F2960E4-A4EE-4F98-8297-136EBD48C24C
P50
description
Forscher
@de
chercheur
@fr
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
研究者
@zh
name
Hayao Taguchi
@en
Taguchi H
@ast
Taguchi H
@es
Taguchi H
@nl
type
label
Hayao Taguchi
@en
Taguchi H
@ast
Taguchi H
@es
Taguchi H
@nl
altLabel
Taguchi H
@en
prefLabel
Hayao Taguchi
@en
Taguchi H
@ast
Taguchi H
@es
Taguchi H
@nl
P31
P496
0000-0001-5270-581X