About: Asp477 is a determinant of the enantioselectivity in yeast transketolase

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About: Asp477 is a determinant of the enantioselectivity in yeast transketolase Goto Sponge NotDistinct Permalink

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scientific article published on 01 March 1998

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 1998 (uk) article scientifique publié en 1998 (fr) im März 1998 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en marzu de 1998 (ast) scientific article published on 01 March 1998 (en)
publication date	wds:Q57396054-3894C5D9-C61B-4977-BA70-C3098491B5EC
publication date	1998-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57396054-78E9C8F7-D81A-4787-B4C3-42CFDD20EA8D
language of work or name	English
cites work	wds:Q57396054-052E11F6-484F-474E-B734-7AD60A38792F wds:Q57396054-070B29B5-C1B9-4924-82EE-FE63AE7C5018 wds:Q57396054-08527C04-F57D-47B0-B940-926C0DB755EE wds:Q57396054-0AD35B87-F783-4A60-8E99-74849D46218B wds:Q57396054-0F732F89-2DE3-4CA6-B554-4FA76FC1B93E wds:Q57396054-2B453CAA-098E-4A6A-AA53-B4426918CB01 wds:Q57396054-3B27F8C9-719E-4FE2-BD6A-55BE0DBACFE1 wds:Q57396054-468E57B7-5312-41C1-8271-4C078AEE72FC wds:Q57396054-6795DB3C-2BC6-40F0-AE86-3CB1926A94C7 wds:Q57396054-67C01721-23A1-4936-8098-0C16EE398775 wds:Q57396054-74BE140F-A482-4C94-A624-4DEB896CAE99 wds:Q57396054-932AB5A1-9AD6-439C-BF6C-629A90A567C7 wds:Q57396054-95DBC41C-290F-4F28-AF2B-445870A45D18 wds:Q57396054-AC52C7C9-7F1A-4B39-A949-684C56B8A030
cites work	Identification of catalytically important residues in yeast transketolase Examination of the Thiamin Diphosphate Binding Site in Yeast Transketolase by Site-Directed Mutagenesis His103 in yeast transketolase is required for substrate recognition and catalysis. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis Enzymes of pentose biosynthesis. The quaternary structure and reacting form of transketolase from baker's yeast Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. Conserved residues are functionally distinct within transketolases of different species Chemical modification of tryptophan at the binding site of thiamine-pyrophosphate in transketolase from baker's yeast Transketolase from yeast, rat liver, and pig liver Three-dimensional structure of apotransketolase flexible loops at the active site enable cofactor binding Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation Synthesis of 3-Deoxy-D-manno-2-octulosonate-8-phosphate (KDO-8-P) fromD-Arabinose: Generation of D-Arabinose-5-Phosphate using Hexokinase
author name string	wds:Q57396054-1BD3F413-C937-4682-B110-7686FABC3A07 wds:Q57396054-3994D9E3-FF14-41EA-9E42-C563701E4BEC wds:Q57396054-7E261247-939E-4801-A769-800FE39844EC wds:Q57396054-D3195687-0849-458B-ACBA-6001BA80FE7A
author name string	U Nilsson C Guerard L Hecquet T Gefflaut
rdfs:label	Asp477 is a determinant of the enantioselectivity in yeast transketolase (en) Asp477 is a determinant of the enantioselectivity in yeast transketolase (nl)
skos:prefLabel	Asp477 is a determinant of the enantioselectivity in yeast transketolase (en) Asp477 is a determinant of the enantioselectivity in yeast transketolase (nl)
name	Asp477 is a determinant of the enantioselectivity in yeast transketolase (en) Asp477 is a determinant of the enantioselectivity in yeast transketolase (nl)
author	wds:Q57396054-FC5AD368-B131-4C80-BE60-E9B49516D590
author	Gunter Schneider
title	wds:Q57396054-8A4288C3-458F-4563-9A91-7A372701FABC
title	Asp477 is a determinant of the enantioselectivity in yeast transketolase (en)
page(s)	wds:Q57396054-E8AD4E9C-FDE3-4747-A888-D7D5B9DAE3E6
page(s)	49-52
instance of	wds:Q57396054-4AB389BE-A2D4-41DB-8961-4CA0EB2B3B7A
instance of	scholarly article
main subject	wds:Q57396054-50BDE5FB-123F-4D1C-A103-F935FBA276E8 wds:Q57396054-BE5C246E-2573-409F-950F-5F5BCFB822CB wds:Q57396054-C397DEF8-1FA1-407B-8CAE-0CFC4B9729E4 wds:Q57396054-C570568E-95A6-4209-94AF-64881D7764CC wds:Q57396054-D46DB6D1-00F9-4D55-A5CD-0EA571DA0214
main subject	cell biology biophysics molecular biology structural biology enantioselectivity
PubMed ID	wds:Q57396054-1E738E83-D337-4438-8AF4-FDA01472AFA6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9537513
PubMed ID	9537513
published in	wds:Q57396054-E133EE72-8DF7-42F7-9534-507B4A768674
published in	FEBS Letters
issue	wds:Q57396054-71662123-99E5-40C7-82A1-0E9755AED846
volume	wds:Q57396054-76CCCB52-8B1C-40C3-B31E-E4D903BA3368
issue	1-2
volume	424
DOI	wds:Q57396054-67676DBC-E8C8-458C-AD23-4A937CA9279C
DOI	http://dx.doi.org/10.1016/S0014-5793(98)00136-7
DOI	10.1016/S0014-5793(98)00136-7
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57396054
is cites work of	Potential use of sugar binding proteins in reactors for regeneration of CO2 fixation acceptor D-Ribulose-1,5-bisphosphate Examination of donor substrate conversion in yeast transketolase Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis. 1-Deoxy-D-xylulose 5-phosphate synthase, the gene product of open reading frame (ORF) 2816 and ORF 2895 in Rhodobacter capsulatus A candidate gene association study on muscat flavor in grapevine (Vitis vinifera L.). A thermostable transketolase evolved for aliphatic aldehyde acceptors Engineering stereoselectivity of ThDP-dependent enzymes Evolutionary analysis of the TPP-dependent enzyme family. Applications of transketolases in organic synthesis. The origin of the absorption band induced through the interaction between apotransketolase and thiamin diphosphate Rational substrate and enzyme engineering of transketolase for aromatics. Enhancement of the substrate scope of transketolase. Identification of an allele of CLA1 associated with variegation in Arabidopsis thaliana
is cites work of	wds:Q24792424-84D7B734-FECB-420E-915B-B04B24EF0782 wds:Q35442895-21BBE974-03C8-4887-8A7F-3A746DF60406 wds:Q44021034-E4E1B7AB-E67A-43EC-B70C-7E8C2702A435

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