About: Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency

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About: Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1996

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rdf:type	Item
description	wetenschappelijk artikel (nl) bài báo khoa học (vi) наукова стаття, опублікована в серпні 1996 (uk) article scientifique publié en 1996 (fr) im August 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'agostu de 1996 (ast) scientific article published on 01 August 1996 (en)
publication date	wds:Q71245490-56609212-14FF-44A0-956B-9F41C98CDB53
publication date	1996-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q71245490-91A9A49F-0EE1-4426-884C-105E55C39ED3
language of work or name	English
cites work	wds:Q71245490-08084DED-4BF0-4B81-916F-47F7DCA63135 wds:Q71245490-0B7E2FF1-AB5A-4E18-A462-6E39B5D23591 wds:Q71245490-0F788D5B-8079-4679-86AB-C1C951483D14 wds:Q71245490-0FED4D05-2414-448D-B11B-3261155C9AC7 wds:Q71245490-23BDE625-7252-45ED-83AD-F97816001B2B wds:Q71245490-458F52DF-5052-488A-85D0-038AEDA95E58 wds:Q71245490-48FA1ACA-03C3-49D7-9B16-F3A6F1229C5C wds:Q71245490-4D55BE21-2D9B-4343-A5B1-AD83E4699383 wds:Q71245490-4E69EAE4-14D8-4448-8E2D-1C6EE5455B06 wds:Q71245490-51DB3135-5BB5-41DD-B166-9067531D6194 wds:Q71245490-597C6C15-E6B8-4035-802C-6833CEF8E0F5 wds:Q71245490-5DA91A85-0697-4B8C-83B7-AA9D2B0B6E45 wds:Q71245490-607020BF-A03E-4296-AA83-D7F5F77C6E35 wds:Q71245490-663EB23F-0A75-4C82-9880-E2EA7D739060 wds:Q71245490-664D1D9C-0870-4A8C-A64D-3FF1029280DF wds:Q71245490-6D785B10-75A4-4F10-BBD1-D12230308908 wds:Q71245490-702AD318-4962-44E7-B5D4-30950E77420F wds:Q71245490-7D3F012E-2C13-4D0A-B037-0A323502030C wds:Q71245490-84DD759C-78AB-4F97-95D7-3F9575EBDDF3 wds:Q71245490-8766DBA1-E346-4C93-B668-00CC6E4D1DFF wds:Q71245490-8E2A4EF0-5F0F-458E-A4BB-BA638BD30659 wds:Q71245490-972F1D27-FFD5-4975-AC96-9A2A298489B2 wds:Q71245490-A86DC415-8B8C-4346-9DA8-0AD9B5B003BB wds:Q71245490-ABB923DB-1D0A-4078-8332-723183CB814C wds:Q71245490-B163CAE9-1B87-49BA-9104-81AEED92C1D3 wds:Q71245490-B8AE1B9D-775A-4359-91EC-A515B45461F8 wds:Q71245490-BF0417D3-F9C7-47E3-BEDD-9547862AD24F wds:Q71245490-C4612CDF-5DBA-4D75-8307-6A1950DD258F wds:Q71245490-C8BFB8F3-9345-483B-A5AE-4C5AACAE3AB5 wds:Q71245490-CE2DC91A-6964-49B7-B9A1-2515EB9F76D7 wds:Q71245490-DBEEE711-272F-41C5-877C-884091AB8ECA wds:Q71245490-DD9BD9BA-220F-47D6-8CE4-6568F1EF19A9 wds:Q71245490-F06CC69C-03EE-461C-992B-8F2965BD8618 wds:Q71245490-F85A1CC8-FEDA-438A-9E93-6849ABE38AE8 wds:Q71245490-FAAE5EE5-2A4D-48AC-A677-0E73DE96CBDF wds:Q71245490-FDF7E084-7B60-4279-9071-75F88AC8F2E2 wds:Q71245490-FE0D2466-DE6C-4D8E-83C5-4A689B75AAF3 wds:Q71245490-FF905313-E293-464F-85F4-E8DBEC4A7CCB
cites work	Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase Development of the particle inflow gun for DNA delivery to plant cells Leucine 332 influences the CO2/O2 specificity factor of ribulose-1,5-bisphosphate carboxylase/oxygenase from Anacystis nidulans Serine-376 contributes to the binding of substrate by ribulose-bisphosphate carboxylase/oxygenase from Anacystis nidulans Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulose-bisphosphate carboxylase/oxygenase Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase A simple and rapid method for the selection of oligodeoxynucleotide-directed mutants. Regulation of Soybean Net Photosynthetic CO(2) Fixation by the Interaction of CO(2), O(2), and Ribulose 1,5-Diphosphate Carboxylase. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogues A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding A role for the epsilon-amino group of lysine-334 of ribulose-1,5-bisphosphate carboxylase in the addition of carbon dioxide to the 2,3-enediol(ate) of ribulose 1,5-bisphosphate. Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase Targeted disruption of chloroplast genes in Chlamydomonas reinhardtii Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas Preparative-scale enzymic synthesis of d-[14C]ribulose 1,5-bisphosphate High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial RubiSCO containing "algal" residue modifications. Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site A Sensitive Assay Procedure for Simultaneous Determination of Ribulose-1,5-bisphosphate Carboxylase and Oxygenase Activities Photosynthesis-deficient Mutants of Chlamydomonas reinhardii with Associated Light-sensitive Phenotypes How various factors influence the CO2/O 2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase Rice chloroplast DNA molecules are heterogeneous as revealed by DNA sequences of a cluster of genes Abscisic acid biosynthesis in roots : I. The identification of potential abscisic acid precursors, and other carotenoids Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form. Sequence of the rbcL gene for the large subunit of ribulose bisphosphate carboxylase-oxygenase from petunia Sequence of the rbcL gene for the large subunit of ribulose bisphosphate carboxylase-oxygenase from alfalfa Mechanistic insights provided by deletion of a flexible loop at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase Complementing amino acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Proteolysis and transition-state-analogue binding of mutant forms of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii Essentiality of Lys-329 of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as demonstrated by site-directed mutagenesis Status of the substrate binding sites of ribulose bisphosphate carboxylase as determined with 2-C-carboxyarabinitol 1,5-bisphosphate.
author name string	wds:Q71245490-773D0483-EDD3-4834-9E38-33C2FFF6829C wds:Q71245490-F4E56427-1852-4838-83A5-23855B56FE7C
author name string	G Zhu R J Spreitzer
rdfs:label	Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (en) Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (nl)
skos:prefLabel	Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (en) Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (nl)
name	Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (en) Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (nl)
title	wds:Q71245490-9E27EFA6-DAB1-42EA-A096-D353347D37EB
title	Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency (en)

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