Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation.
about
Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilaneStructure of human porphobilinogen deaminase at 2.8 A: the molecular basis of acute intermittent porphyriaInsights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzymeUnique properties of Plasmodium falciparum porphobilinogen deaminaseStructure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic sitePorphobilinogen deaminase gene structure and molecular defectsMolecular basis of acute intermittent porphyria: mutations and polymorphisms in the human hydroxymethylbilane synthase genePorphobilinogen deaminase and uroporphyrinogen III synthase: structure, molecular biology, and mechanismTime-resolved and static-ensemble structural chemistry of hydroxymethylbilane synthaseCharacterization of two isoalleles and three mutations in both isoforms of purified recombinant human porphobilinogen deaminase.Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria.Functions of the gene products of Escherichia coli.The common origins of the pigments of life-early steps of chlorophyll biosynthesis.The three-dimensional structures of mutants of porphobilinogen deaminase: toward an understanding of the structural basis of acute intermittent porphyria.Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana.Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria.The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme.Human hydroxymethylbilane synthase: Molecular dynamics of the pyrrole chain elongation identifies step-specific residues that cause AIP.Structural basis of pyrrole polymerization in human porphobilinogen deaminase
P2860
Q27322988-ADD4A47C-29B1-46BC-8446-1FDA2FC45EFAQ27653713-407F84FE-7B3C-44C7-BEEE-301341160AD8Q27684243-F2C3D422-F66D-4231-B24B-EC557A233C78Q27974466-F03CAD48-0464-40B5-B9EA-F855036534FEQ28269612-95005957-775D-4BF9-8E80-885674CCC105Q28291727-76520E1B-335E-4836-8A18-B70C97F3A250Q28307580-119B2762-1713-4E5C-BB76-D25B24165E92Q28678722-732B1FE5-69B8-45FA-8D58-603D7B79710AQ29026558-3AEF4E57-BCA6-4983-B3B7-7069D491C803Q33219744-34971E5D-4E1A-4514-9B19-09B5E3F571ACQ35250368-06B685DC-E3A2-4251-967F-D003D0AA7F6FQ37059813-7F31FB99-CE6D-48B9-ACFE-0BB6156B7EB8Q38168775-D48C3BBC-201D-4346-B1FF-164342484F5FQ40588503-D31432C3-FA6C-4837-A9F0-C1A048BA4A0DQ42086544-E16E13AF-788A-477D-A62C-17C2233908EDQ42546208-08F33E41-5563-487D-BBDA-AFD39EF0F123Q42635059-14F5E20F-220E-4A22-8AFD-9B54BBC8CD28Q42982351-1EA85744-C78C-46F3-93B4-408D22EAF147Q52597879-7C6C0D8A-2127-491B-A45B-D8A5379341ABQ58038918-E7775C9B-086D-4ADF-89CF-D5B45498BCEE
P2860
Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Mutagenesis of arginine residu ...... ain initiation and elongation.
@en
Mutagenesis of arginine residu ...... ain initiation and elongation.
@nl
type
label
Mutagenesis of arginine residu ...... ain initiation and elongation.
@en
Mutagenesis of arginine residu ...... ain initiation and elongation.
@nl
prefLabel
Mutagenesis of arginine residu ...... ain initiation and elongation.
@en
Mutagenesis of arginine residu ...... ain initiation and elongation.
@nl
P2860
P356
P1433
P1476
Mutagenesis of arginine residu ...... ain initiation and elongation.
@en
P2093
Woodcock SC
P2860
P304
P356
10.1042/BJ2800445
P407
P478
280 ( Pt 2)
P577
1991-12-01T00:00:00Z