The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.
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Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilaneStructural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of theBacillus megateriumenzyme at near-atomic resolutionInsights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzymeTime-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthaseRegulation of the tetrapyrrole biosynthetic pathway leading to heme and chlorophyll in plants and cyanobacteria.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana.Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals.Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium.Acute intermittent porphyria in Sweden. Molecular, functional and clinical consequences of some new mutations found in the porphobilinogen deaminase gene.Acute intermittent porphyria--impact of mutations found in the hydroxymethylbilane synthase gene on biochemical and enzymatic protein properties.Human hydroxymethylbilane synthase: Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP.
P2860
Q27322988-76775126-914A-46B6-BD2D-C2975344DEE7Q27681997-D6AAF397-5C67-4F83-9CDA-BBE25BAF53C9Q27684243-9E322256-09B9-4FD2-858F-64671D80F418Q29026558-D280FE08-F12B-4A52-A521-776D5367178EQ34637195-437D2E1F-B68F-4BEA-9C86-69DF8F2F2D98Q39103477-E66486F4-BEC9-4AB6-A7CC-657F2A85968AQ41813453-BB61C1F5-2ADF-4CC2-A65A-AD2E201ED6CDQ42846029-E89B0554-CFAE-44E7-806B-DF858CCD3914Q43066463-DE775915-C49B-45EF-8A94-5AE792F6C7AAQ44173479-F20C8914-C1CD-4D74-BB7F-48D8AAC8F034Q45775369-0D2F087F-7464-403B-97E3-1987EF756825Q52597879-7C1B684F-5FC9-4196-AEEF-D5A2878698CC
P2860
The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@en
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@nl
type
label
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@en
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@nl
prefLabel
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@en
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@nl
P2093
P2860
P1433
P1476
The three-dimensional structur ...... eaminase at 1.76-A resolution.
@en
P2093
Brownlie PD
Malashkevich VN
Shoolingin-Jordan PM
P2860
P356
10.1002/(SICI)1097-0134(199605)25:1<48::AID-PROT5>3.0.CO;2-G
P407
P577
1996-05-01T00:00:00Z