About: Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium

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description	artículu científicu espublizáu en 2000 (ast) vědecký článek publikovaný v roce 2000 (cs) 2000 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в травні 2000 (uk) 2000 թվականի մայիսին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 2000/05/12) (sk) مقالة علمية (نشرت في 12-5-2000) (ar) wetenschappelijk artikel (gepubliceerd op 2000/05/12) (nl) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im Mai 2000 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28489056-4A298A5E-CB9D-4BD8-BC71-0F6EDAADF157
publication date	2000-05-12 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28489056-D3F1DF8C-1335-4D8F-9296-BA979F2A3AD4
language of work or name	English
cites work	wds:Q28489056-00BB4B41-8206-4438-BC4B-89F2AE9868B5 wds:Q28489056-1D727A4E-DE38-4A4D-987A-BF59BCF3F300 wds:Q28489056-2881C96D-DDD5-45BD-A926-317F424EC2F1 wds:Q28489056-2B9A08C5-6F51-41CD-88EF-277FF8501095 wds:Q28489056-2DE7D646-A6A0-4863-8C11-7C21B45CD5C8 wds:Q28489056-33ECB15B-EF58-42A7-8F5F-7BE3FDA7621B wds:Q28489056-3ABA45A3-CCA4-4208-8717-F4EF96AB5AFD wds:Q28489056-3B063B10-3F0B-4522-8B9B-1B4361A0DD88 wds:Q28489056-3E4B7954-B0D6-497D-82CD-A1A14F6660B0 wds:Q28489056-3ED3CF8F-2F84-4127-9C08-4625DFDA6DC1 wds:Q28489056-43FB9F21-35D9-416E-B482-E4C81255673E wds:Q28489056-49E6F8A5-31D0-453C-B9A7-F597AA3D26BC wds:Q28489056-59A65D75-79EC-4F6F-B5BA-6F2D73C513CF wds:Q28489056-6D615089-2D57-495D-94B0-7C524CA79C17 wds:Q28489056-703E15F0-9D82-41E5-BB31-A2D9D80FFE69 wds:Q28489056-7709FA91-2F1A-4E1D-BFF7-E78A5CF9DAC1 wds:Q28489056-7C829F0A-EBBB-4DD3-973C-9DB9BE72CA69 wds:Q28489056-7E765A14-F4EA-4841-8C05-7E7DB93819AD wds:Q28489056-D5773124-CEBC-4A4C-BA0A-A9A4A8912452 wds:Q28489056-D7C0ACD6-5C92-4008-99A5-6ED145CB1E38 wds:Q28489056-E75F75F3-3C39-4753-8FBC-EC6D3B78CA52 wds:Q28489056-EFDB04FF-C1E4-4C53-AC74-A4BCA03DFCB0 wds:Q28489056-F36BAEEA-A726-475D-B7B7-BA87E5F648FF wds:Q28489056-FDDE4365-4D72-452E-8932-29318E811C89
cites work	Sequence Analysis of the Genome of the Unicellular Cyanobacterium Synechocystis sp. Strain PCC6803. II. Sequence Determination of the Entire Genome and Assignment of Potential Protein-coding Regions Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenases from mustard (Sinapis alba). The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation Identification, sequence analysis, and expression of a Corynebacterium glutamicum gene cluster encoding the three glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomerase Measurement of protein by spectrophotometry at 205 nm. The complete genome sequence of the gram-positive bacterium Bacillus subtilis Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis 5'-noncoding region sacR is the target of all identified regulation affecting the levansucrase gene in Bacillus subtilis Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis Plasmids for ectopic integration in Bacillus subtilis. A vector for systematic gene inactivation in Bacillus subtilis Control of the shift from homolactic acid to mixed-acid fermentation in Lactococcus lactis: predominant role of the NADH/NAD+ ratio Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+ Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the fingerprint region of the nucleotide binding fold. Involvement of pyruvate dehydrogenase in product formation in pyruvate-limited anaerobic chemostat cultures of Enterococcus faecalis NCTC 775. Carbon-flux distribution in the central metabolic pathways of Corynebacterium glutamicum during growth on fructose Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. An operon encoding three glycolytic enzymes in Lactobacillus delbrueckii subsp. bulgaricus: glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase. Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. The glyceraldehyde-3-phosphate dehydrogenase of Clostridium acetobutylicum: isolation and purification of the enzyme, and sequencing and localization of the gap gene within a cluster of other glycolytic genes Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (gap) is developmentally regulated and induced by glucose.
author name string	wds:Q28489056-1427552D-CEFB-47B6-BFD9-669D3F266F4C wds:Q28489056-1EAB14F7-4FE4-490B-8088-F2A7520CEA83 wds:Q28489056-3DB88D32-3D5D-4FBE-83B8-B9A90D826C82 wds:Q28489056-4631FE1E-24C3-4707-B751-A25E1DCA3152 wds:Q28489056-B706C451-792A-4987-A785-D79ECB3A80D0 wds:Q28489056-E0953770-BB31-4387-86E0-82B26CA88697
OpenCitations bibliographic resource ID	wds:Q28489056-AFC07517-D632-490B-8224-CE8BE7596644
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2791188
author name string	G. Branlant E. Dervyn S. Aymerich S. Azza S. Boschi-Muller S. Fillinger
OpenCitations bibliographic resource ID	2791188
rdfs:label	Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (en) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (nl) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (ast)
skos:prefLabel	Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (en) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (nl) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (ast)
name	Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (en) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (nl) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (ast)
title	wds:Q28489056-98CFCB9F-54D6-48CD-994E-8F5A45D076ED
title	Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium (en)
page(s)	wds:Q28489056-DF4A51A2-3200-4715-98E5-504E05D1A72D
page(s)	14031–14037
instance of	wds:Q28489056-61FE6796-5C86-4EAB-927A-D38E5B531506
instance of	scholarly article
PubMed ID	wds:Q28489056-79AED483-6255-41B3-A746-4E219EF5B747
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10799476
PubMed ID	10799476
published in	wds:Q28489056-DED7C751-F34E-4258-A15E-4B143511AACD
published in	Journal of Biological Chemistry
issue	wds:Q28489056-F5C0A6D7-DCB3-4EC5-9C0B-79DAA66F4417

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