High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
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The molecular mechanism of lead inhibition of human porphobilinogen synthaseAllostery and the dynamic oligomerization of porphobilinogen synthaseShape shifting leads to small-molecule allosteric drug discoveryRhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamerMolecular evolution of multiple-level control of heme biosynthesis pathway in animal kingdomThe X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitorsCrystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanismSpecies-specific inhibition of porphobilinogen synthase by 4-oxosebacic acidX-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydrataseControl of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthaseStructure of the Heme Biosynthetic Pseudomonas aeruginosa Porphobilinogen Synthase in Complex with the Antibiotic AlaremycinCrystal Structure of Toxoplasma gondii Porphobilinogen SynthaseDetecting coevolution in and among protein domainsSubstrate-induced interconversion of protein quaternary structure isoforms.Regulation of the tetrapyrrole biosynthetic pathway leading to heme and chlorophyll in plants and cyanobacteria.Probing the oligomeric assemblies of pea porphobilinogen synthase by analytical ultracentrifugationwALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.Structure and function of enzymes in heme biosynthesis.Recent advances in the biosynthesis of modified tetrapyrroles: the discovery of an alternative pathway for the formation of heme and heme d 1.An artificial gene for human porphobilinogen synthase allows comparison of an allelic variation implicated in susceptibility to lead poisoning.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase.Delta-aminolevulinic acid dehydratase from Plasmodium falciparum: indigenous versus imported.Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris Hildenborough.Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.The Remarkable Character of Porphobilinogen Synthase.Single amino acid mutations alter the distribution of human porphobilinogen synthase quaternary structure isoforms (morpheeins).A structural basis for half-of-the-sites metal binding revealed in Drosophila melanogaster porphobilinogen synthase.
P2860
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P2860
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@ast
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@en
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@nl
type
label
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@ast
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@en
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@nl
prefLabel
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@ast
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@en
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@nl
P2093
P356
P1476
High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase
@en
P2093
J B Cooper
N Frankenberg
P M Shoolingin-Jordan
P T Erskine
P304
P356
10.1006/JMBI.1999.2808
P407
P50
P577
1999-06-01T00:00:00Z