About: Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis

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About: Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2003 (ast) vědecký článek publikovaný v roce 2003 (cs) 2003 թվականի օգոստոսին հրատարակված գիտական հոդված (hy) 2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в серпні 2003 (uk) 2003年學術文章 (zh) مقالة علمية (نشرت في أغسطس 2003) (ar) vedecký článok (publikovaný 2003/08/01) (sk) wetenschappelijk artikel (gepubliceerd op 2003/08/01) (nl) im August 2003 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28490053-53FAF976-E743-4ACE-9BAE-EA6EF09E0927
publication date	2003-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28490053-D5B7D16E-98B5-430A-9D50-A57B92FACBF1
language of work or name	English
cites work	wds:Q28490053-03501B80-B472-4210-AF1A-C303287BC698 wds:Q28490053-0704272C-5CAC-44CF-A804-5CD89323D305 wds:Q28490053-09D36738-C623-4D87-86D3-E11E4C9B5320 wds:Q28490053-0A4774A7-6FD3-485E-9C5D-EFA86E5D14B8 wds:Q28490053-0B3AB7E1-E4B6-4F12-B5ED-711BB61FB137 wds:Q28490053-124F60E5-D3FD-4A0C-8A0B-788DA8C87A90 wds:Q28490053-1794548E-AC46-49D5-A10A-9ADC9B4C10C4 wds:Q28490053-1B06EEC6-43D4-427F-AFCA-B6F4D566F4C4 wds:Q28490053-235A8400-40A7-4651-A6C1-6B7F81D04621 wds:Q28490053-2B923B74-AA8E-4AD8-9D72-8CD9A5B275CC wds:Q28490053-34FD65D4-288F-4D62-8F32-C6118D3ECF77 wds:Q28490053-365BB40E-8DA1-4C6D-A39D-5856E7BCC1C2 wds:Q28490053-3F3F3184-054D-4B8B-9398-61D620B77DD5 wds:Q28490053-443E0FE2-FEE2-4EDD-B666-BFA61427589D wds:Q28490053-44679336-5080-4062-B54A-4F4787315D6C wds:Q28490053-490EBE3E-4AF8-4E1A-82D8-C7985C3D7D81 wds:Q28490053-4ADE4A7E-6CA1-490F-9A31-E257F3263256 wds:Q28490053-51309D87-AF82-4821-B316-2F0BB718C1C3 wds:Q28490053-52F3C649-103A-4CED-B552-3A37CD8838D9 wds:Q28490053-5B45AEC6-793E-41AA-B3DC-5F7803D2E800 wds:Q28490053-5BB885AE-323F-4A18-973F-583874CD0A59 wds:Q28490053-78CA66EA-F1BC-46A4-90E7-21E1D20F5AC4 wds:Q28490053-791C84CD-E995-4B06-9D17-F8E35C1FD64B wds:Q28490053-845B406E-6CED-40C4-83EB-1D10A97CF943 wds:Q28490053-9008FFC4-B976-4BA3-A1EE-403EDC79D04D wds:Q28490053-98CCC97F-9808-490B-8154-BE111DBBB6AB wds:Q28490053-A60D9938-5982-4A84-B8CB-462FDEEADFFD wds:Q28490053-B9A0F96F-2326-444A-B3F0-940AD18A608C wds:Q28490053-BAE2A3CE-04FA-4D3E-85E2-EE66F59AB785 wds:Q28490053-C38D74DC-EE16-4E77-96FF-594B21FB73C5 wds:Q28490053-C443A110-4B42-49F3-8FFC-92A54595B0B9 wds:Q28490053-D5F7DD52-4761-4EE3-B0E5-0E59D151F51A wds:Q28490053-D708F192-F1E8-4C3C-9E8F-0900C22A1C52 wds:Q28490053-F061FD58-2E44-4265-A013-269C3D1AD786 wds:Q28490053-F129BB4C-5D2E-4790-8B14-60A678580B25
cites work	Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Basic local alignment search tool The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis Procedure for Identifying Nonsense Mutations Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Transformation in restriction-deficient Salmonella typhimurium LT2. Carboxyphosphonoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans The structure and domain organization of Escherichia coli isocitrate lyase Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants Crystal Structure of 2-Methylisocitrate Lyase (PrpB) from Escherichia coli and Modelling of its Ligand Bound Active Centre Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes Alkylation of isocitrate lyase from Escherichia coli by 3-bromopyruvate. Propionate catabolism in Salmonella typhimurium LT2: two divergently transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a member of the sigma-54 family of activators, and the prpBCDE genes constitute an operon In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate Studies of regulation of expression of the propionate (prpBCDE) operon provide insights into how Salmonella typhimurium LT2 integrates its 1,2-propanediol and propionate catabolic pathways The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. Comparative structure, function and regulation of isocitrate lyase, an important assimilatory enzyme Inhibition of isocitrate lyase by 3-nitropropionate, a reaction-intermediate analogue Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification Quick transformation in Salmonella typhimurium LT2. Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site Identification of a cysteine residue at the active site of Escherichia coli isocitrate lyase Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli.
author name string	wds:Q28490053-31C1C949-C8E5-4EAE-AB00-BA1262969DDC wds:Q28490053-4E6E68B7-C473-446F-8C19-0710B774F65A wds:Q28490053-9AD26555-C3E4-4B19-96DF-0E2306F4BC8F
author name string	J C Escalante-Semerena H Holden T L Grimek
rdfs:label	Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (en) Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (nl) Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (ast)
skos:prefLabel	Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (en) Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (nl) Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (ast)
name	Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (en) Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis (nl)

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