About: Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 April 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im April 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована у квітні 2000 (uk) im April 2000 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en avril 2000 (fr) artículu científicu espublizáu n'abril de 2000 (ast) scientific article published on 01 April 2000 (en)
publication date	wds:Q73790229-EC300B58-494B-45E4-AA37-53D5DB23B123
publication date	2000-04-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q73790229-AE9C06CC-A296-448D-A6BC-05C757B388F6 wds:Q73790229-E6E61ABF-FE00-492B-8CA4-69C91F4A842D wds:Q73790229-F9C6E104-6229-47E5-9104-4B4202F5104E
author name string	J G Zeikus C Vieille D Sriprapundh
rdfs:label	Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (en) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (nl)
skos:prefLabel	Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (en) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (nl)
name	Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (en) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (nl)
title	wds:Q73790229-A6E937D7-53B1-48F1-9D47-508429055FCC
title	Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis (en)
page(s)	wds:Q73790229-F4ED252C-19C8-4E8D-A5C0-E2E11669062E
page(s)	259-265
instance of	wds:Q73790229-6F22A549-7E14-40DA-9EF1-214AE01C1865
instance of	scholarly article
PubMed ID	wds:Q73790229-DD7E3A5A-8658-4842-91AB-F231086FEE05
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10810157
PubMed ID	10810157
published in	wds:Q73790229-3072EEB6-8A3B-497A-B201-F35209979C5C
published in	Protein Engineering Design and Selection
issue	wds:Q73790229-9796063F-71C1-4281-8C0A-F70D656B4611
volume	wds:Q73790229-0A9190CC-DE69-43C2-AE35-82D1815425FA
issue	4
volume	13
DOI	wds:Q73790229-BF9F5FAA-4FCC-4798-97BD-7F1EF450270B
DOI	http://dx.doi.org/10.1093/PROTEIN/13.4.259
DOI	10.1093/PROTEIN/13.4.259
describes a project that uses	wds:Q73790229-695857B5-F7AB-4221-B688-F4008744C217
describes a project that uses	site-directed mutagenesis
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73790229
is cites work of	Directed evolution of xylose isomerase for improved xylose catabolism and fermentation in the yeast Saccharomyces cerevisiae Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently Selection of mutations for increased protein stability Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus Improved thermostability of an acidic xylanase from Aspergillus sulphureus by combined disulphide bridge introduction and proline residue substitution The contribution of proline residues to protein stability is associated with isomerization equilibrium in both unfolded and folded states Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution Insertion of endocellulase catalytic domains into thermostable consensus ankyrin scaffolds: effects on stability and cellulolytic activity Improvement and characterization of a hyperthermophilic glucose isomerase from Thermoanaerobacter ethanolicus and its application in production of high fructose corn syrup. Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability. Enhancement of stability of immobilized glucose oxidase by modification of free thiols generated by reducing disulfide bonds and using additives Structural Basis for Thermostability of -Glycosidase from the Thermophilic Eubacterium Thermus nonproteolyticus HG102 Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two hyperthermophilic Thermotoga species Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II Optimization of a β-sheet-cap for long loop closure Expression of a Recombinant Anti-HIV and Anti-Tumor Protein, MAP30, in Nicotiana tobacum Hairy Roots: A pH-Stable and Thermophilic Antimicrobial Protein Conformational thermostabilisation of corticotropin releasing factor receptor 1. Thermostabilization of the uronate dehydrogenase from Agrobacterium tumefaciens by semi-rational design. N-terminal fusion of a hyperthermophilic chitin-binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes A theoretical model of Aquifex pyrophilus flagellin: implications for its thermostability. Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites A Novel Glucose Isomerase from Caldicellulosiruptor bescii with Great Potentials in the Production of High-Fructose Corn Syrup Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase Purification and kinetic behavior of glucose isomerase from Streptomyces lividans RSU26 Thermostabilization of VPR, a kinetically stable cold adapted subtilase, via multiple proline substitutions into surface loops
is cites work of	wds:Q30401796-8B09903D-48D7-4A34-A154-960080ED09ED wds:Q34365202-EF904E1E-953A-4575-ABC3-43B34CB9118E wds:Q49244090-765FAE41-340C-4460-8838-9214600595D0 wds:Q39324214-CA176035-3EFD-4C7D-B748-F26D2D3846B2 wds:Q36085956-E15BA6D1-090D-4DCD-B6E1-57D727B3C9E4 wds:Q42119832-77F4C31D-F1CC-478B-B258-6ED3C4566ADC wds:Q28649577-7D4678DA-0215-45D2-A757-0D1F59D7F9A0 wds:Q38287400-A7216C75-8815-471F-AFAD-8AA58B245945 wds:Q30746506-A8BD2E5D-C8C6-4535-8CE0-14B4326A3387 wds:Q42248900-4E947DBD-BAE3-4131-974A-1A7DD870538D wds:Q44698400-269AD9B5-9BAA-434F-89B1-6CC7827A5838 wds:Q27656532-C0B87A0F-03C5-4EF6-AB19-7289A1028E1D wds:Q34147536-42EE7B10-F26B-4D98-93D8-24AD5A9725BE wds:Q90012449-2AF23F71-065E-476B-8CC5-B6C20F9DAADE wds:Q94465815-5B7769D7-FC8B-453E-9B88-63D9042F4D81 wds:Q27641601-73A0CF41-E59B-4A6B-B2F6-BFCD553A0BC9 wds:Q35210215-61C24801-3DF1-44DA-BE94-D0FA5ED64DF2 wds:Q44399553-5855E171-FB50-4874-A724-0F6C800D4F33 wds:Q38298296-F59AD442-0D77-4839-8308-13096725031F wds:Q50084448-E6C1DF30-4A18-4819-AC44-74ADB8B33ED0 wds:Q91633812-92F5155B-0673-43BD-9EDB-F4D919527E6A wds:Q43026375-85B306FE-DC46-4558-9798-3253ED3F0527 wds:Q92890174-290FFB9A-8DCA-44F1-AA06-3B25CC8308CA wds:Q28203641-54FB3CF1-A1C3-43A7-8FD7-352C6D1417B1 wds:Q37011312-534E5881-E132-4EA6-A910-9D8423617F24 wds:Q39639942-48ECAD44-2EBB-4688-9F4B-A561A0E858EE wds:Q42115073-834AD336-9397-47EE-B4DF-A7633AA547A5 wds:Q41151319-3789CDC9-DCB0-4964-8E3D-D79E41464A2A

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software