V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.
about
Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation.Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator proteinInsights into phycoerythrobilin biosynthesis point toward metabolic channeling.Identification and characterization of the terminal enzyme of siroheme biosynthesis from Arabidopsis thaliana: a plastid-located sirohydrochlorin ferrochelatase containing a 2FE-2S center.Accumulation of heme biosynthetic intermediates contributes to the antibacterial action of the metalloid tellurite.On the necessity of dissecting sequence similarity scores into segment-specific contributions for inferring protein homology, function prediction and annotation.Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit.Mg-protoporphyrin IX and heme control HEMA, the gene encoding the first specific step of tetrapyrrole biosynthesis, in Chlamydomonas reinhardtii.The archaeal transamidosome for RNA-dependent glutamine biosynthesis.Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate.Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.Tetrapyrrole Metabolism in Arabidopsis thaliana.tRNA synthetase paralogs: evolutionary links in the transition from tRNA-dependent amino acid biosynthesis to de novo biosynthesisThe Non-canonical Tetratricopeptide Repeat (TPR) Domain of Fluorescent (FLU) Mediates Complex Formation with Glutamyl-tRNA Reductase.dissectHMMER: a HMMER-based score dissection framework that statistically evaluates fold-critical sequence segments for domain fold similarity.Impact of the bacterial type I cytochrome c maturation system on different biological processes.The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein.Aminoacyl-tRNAs, the bacterial cell envelope, and antibioticsSynthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors.New insights in the topology of the biosynthesis of 5-aminolevulinic acid.Crystal structure of glutamate-1-semialdehyde-2,1-aminomutase from Arabidopsis thalianaStructure and function of enzymes in heme biosynthesis.Siroheme: an essential component for life on earth.Thiol-based redox control of enzymes involved in the tetrapyrrole biosynthesis pathway in plants.Recent advances in the biosynthesis of modified tetrapyrroles: the discovery of an alternative pathway for the formation of heme and heme d 1.Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase.Physical and kinetic interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase of Chlamydomonas reinhardtii.Organization of chlorophyll biosynthesis and insertion of chlorophyll into the chlorophyll-binding proteins in chloroplasts.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis.Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU.Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution.tRNA recognition by glutamyl-tRNA reductase.Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis.An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts.Staphylococcus aureus HemX Modulates Glutamyl-tRNA Reductase Abundance To Regulate Heme Biosynthesis.The catalytic subunit of magnesium-protoporphyrin IX monomethyl ester cyclase forms a chloroplast complex to regulate chlorophyll biosynthesis in rice.The 2-thiouridylase function of the human MTU1 (TRMU) enzyme is dispensable for mitochondrial translation.Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.
P2860
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P2860
V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
V-shaped structure of glutamyl ...... dent tetrapyrrole biosynthesis
@nl
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@ast
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@en
type
label
V-shaped structure of glutamyl ...... dent tetrapyrrole biosynthesis
@nl
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@ast
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@en
prefLabel
V-shaped structure of glutamyl ...... dent tetrapyrrole biosynthesis
@nl
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@ast
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@en
P2093
P2860
P356
P1433
P1476
V-shaped structure of glutamyl ...... ent tetrapyrrole biosynthesis.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.23.6583
P407
P577
2001-12-01T00:00:00Z