about
The AAA+ superfamily of functionally diverse proteinsThe structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase.Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhereThe role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and cobalamin biosynthesisGenome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotesMolecular signatures for the main phyla of photosynthetic bacteria and their subgroups.Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement of Mg-chelatase H subunit in plastid-to-nucleus signal transduction.Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers.A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea.The CoxD protein, a novel AAA+ ATPase involved in metal cluster assembly: hydrolysis of nucleotide-triphosphates and oligomerization.Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus.Regulation of the tetrapyrrole biosynthetic pathway leading to heme and chlorophyll in plants and cyanobacteria.Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium.Molecular basis for semidominance of missense mutations in the XANTHA-H (42-kDa) subunit of magnesium chelataseIn planta transient expression as a system for genetic and biochemical analyses of chlorophyll biosynthesis.Tetrapyrrole Metabolism in Arabidopsis thaliana.In vacuo interfacial tetrapyrrole metallation.Efficient Virus-Induced Gene Silencing in Solanum rostratum.Involvement of tetrapyrroles in inter-organellar signaling in plants and algae.Signaling pathways from the chloroplast to the nucleus.Roles of the different components of magnesium chelatase in abscisic acid signal transduction.Chlorophyll biosynthesis gene evolution indicates photosystem gene duplication, not photosystem merger, at the origin of oxygenic photosynthesisRecent overview of the Mg branch of the tetrapyrrole biosynthesis leading to chlorophylls.Mg-chelatase of tobacco: the role of the subunit CHL D in the chelation step of protoporphyrin IX.Abscisic acid receptors: multiple signal-perception sitesRole of magnesium in carbon partitioning and alleviating photooxidative damage.Metal trafficking: from maintaining the metal homeostasis to future drug design.Abscisic acid receptors: past, present and future.Structure and organization of a 25 kbp region of the genome of the photosynthetic green sulfur bacterium Chlorobium vibrioforme containing Mg-chelatase encoding genes.S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase from Rhodobacter capsulatus: mechanistic insights and stimulation with phospholipids.Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells.Genome-based examination of chlorophyll and carotenoid biosynthesis in Chlamydomonas reinhardtii.Factors controlling the reactivity of divalent metal ions towards pheophytin aIdentification and molecular characterization of a novel Chlamydomonas reinhardtii mutant defective in chlorophyll biosynthesis.Identification and molecular characterization of the second Chlamydomonas gun4 mutant, gun4-II.Limitation of nocturnal import of ATP into Arabidopsis chloroplasts leads to photooxidative damage.Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.).BchJ and BchM interact in a 1 : 1 ratio with the magnesium chelatase BchH subunit of Rhodobacter capsulatus.Determinants of catalytic activity with the use of purified I, D and H subunits of the magnesium protoporphyrin IX chelatase from Synechocystis PCC6803.Kinetic analyses of the magnesium chelatase provide insights into the mechanism, structure, and formation of the complex.
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Mechanism and regulation of Mg-chelatase
@ast
Mechanism and regulation of Mg-chelatase
@en
Mechanism and regulation of Mg-chelatase
@en-gb
Mechanism and regulation of Mg-chelatase
@nl
type
label
Mechanism and regulation of Mg-chelatase
@ast
Mechanism and regulation of Mg-chelatase
@en
Mechanism and regulation of Mg-chelatase
@en-gb
Mechanism and regulation of Mg-chelatase
@nl
prefLabel
Mechanism and regulation of Mg-chelatase
@ast
Mechanism and regulation of Mg-chelatase
@en
Mechanism and regulation of Mg-chelatase
@en-gb
Mechanism and regulation of Mg-chelatase
@nl
P2860
P3181
P356
P1433
P1476
Mechanism and regulation of Mg-chelatase
@en
P2093
C J Walker
R D Willows
P2860
P304
P3181
P356
10.1042/BJ3270321
P407
P478
327 ( Pt 2)
P577
1997-10-15T00:00:00Z