152 related articles for article (PubMed ID: 3421931)
1. Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.
Hart GJ; Miller AD; Battersby AR
Biochem J; 1988 Jun; 252(3):909-12. PubMed ID: 3421931
[TBL] [Abstract][Full Text] [Related]
2. Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.
Miller AD; Hart GJ; Packman LC; Battersby AR
Biochem J; 1988 Sep; 254(3):915-8. PubMed ID: 3196304
[TBL] [Abstract][Full Text] [Related]
3. Identification of a cysteine residue as the binding site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase.
Jordan PM; Warren MJ; Williams HJ; Stolowich NJ; Roessner CA; Grant SK; Scott AI
FEBS Lett; 1988 Aug; 235(1-2):189-93. PubMed ID: 3042456
[TBL] [Abstract][Full Text] [Related]
4. Reconstitution of apo-porphobilinogen deaminase: structural changes induced by cofactor binding.
Scott AI; Clemens KR; Stolowich NJ; Santander PJ; Gonzalez MD; Roessner CA
FEBS Lett; 1989 Jan; 242(2):319-24. PubMed ID: 2644132
[TBL] [Abstract][Full Text] [Related]
5. Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.
Jordan PM; Berry A
Biochem J; 1981 Apr; 195(1):177-81. PubMed ID: 6975621
[TBL] [Abstract][Full Text] [Related]
6. Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase.
Warren MJ; Jordan PM
Biochemistry; 1988 Dec; 27(25):9020-30. PubMed ID: 3069132
[TBL] [Abstract][Full Text] [Related]
7. Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase.
Jordan PM; Warren MJ
FEBS Lett; 1987 Dec; 225(1-2):87-92. PubMed ID: 3079571
[TBL] [Abstract][Full Text] [Related]
8. Availability of porphobilinogen controls appearance of porphobilinogen deaminase activity in Escherichia coli K-12.
Umanoff H; Russell CS; Cosloy SD
J Bacteriol; 1988 Oct; 170(10):4969-71. PubMed ID: 3049558
[TBL] [Abstract][Full Text] [Related]
9. Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12.
Jordan PM; Thomas SD; Warren MJ
Biochem J; 1988 Sep; 254(2):427-35. PubMed ID: 3052434
[TBL] [Abstract][Full Text] [Related]
10. Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme.
Shoolingin-Jordan PM; Warren MJ; Awan SJ
Biochem J; 1996 Jun; 316 ( Pt 2)(Pt 2):373-6. PubMed ID: 8687374
[TBL] [Abstract][Full Text] [Related]
11. Site-directed mutagenesis and high-resolution NMR spectroscopy of the active site of porphobilinogen deaminase.
Scott AI; Roessner CA; Stolowich NJ; Karuso P; Williams HJ; Grant SK; Gonzalez MD; Hoshino T
Biochemistry; 1988 Oct; 27(21):7984-90. PubMed ID: 3069124
[TBL] [Abstract][Full Text] [Related]
12. Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics.
Williams DC; Morgan GS; McDonald E; Battersby AR
Biochem J; 1981 Jan; 193(1):301-10. PubMed ID: 6796041
[TBL] [Abstract][Full Text] [Related]
13. The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.
Louie GV; Brownlie PD; Lambert R; Cooper JB; Blundell TL; Wood SP; Malashkevich VN; Hädener A; Warren MJ; Shoolingin-Jordan PM
Proteins; 1996 May; 25(1):48-78. PubMed ID: 8727319
[TBL] [Abstract][Full Text] [Related]
14. Determination of erythrocyte hydroxymethylbilane synthase activity and its application for study of acute intermittent porphyria.
Lee FY; Hsiao KJ; Tsai YT; Lee SD; Wu SJ; Jeng HS
Taiwan Yi Xue Hui Za Zhi; 1988 Nov; 87(11):1029-35. PubMed ID: 3235962
[No Abstract] [Full Text] [Related]
15. Spectroscopic evidence for a porphobilinogen deaminase-tetrapyrrole complex that is an intermediate in the biosynthesis of uroporphyrinogen III.
Rosé S; Frydman RB; de los Santos C; Sburlati A; Valasinas A; Frydman B
Biochemistry; 1988 Jun; 27(13):4871-9. PubMed ID: 3262369
[TBL] [Abstract][Full Text] [Related]
16. Evidence that pyridoxal phosphate modification of lysine residues (Lys-55 and Lys-59) causes inactivation of hydroxymethylbilane synthase (porphobilinogen deaminase).
Miller AD; Packman LC; Hart GJ; Alefounder PR; Abell C; Battersby AR
Biochem J; 1989 Aug; 262(1):119-24. PubMed ID: 2510713
[TBL] [Abstract][Full Text] [Related]
17. Dipyrromethane cofactor assembly in porphobilinogen deaminase.
McNeill LA; Shoolingin-Jordan PM
Biochem Soc Trans; 1998 Aug; 26(3):S286. PubMed ID: 9766005
[No Abstract] [Full Text] [Related]
18. Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution.
Azim N; Deery E; Warren MJ; Wolfenden BA; Erskine P; Cooper JB; Coker A; Wood SP; Akhtar M
Acta Crystallogr D Biol Crystallogr; 2014 Mar; 70(Pt 3):744-51. PubMed ID: 24598743
[TBL] [Abstract][Full Text] [Related]
19. Biosynthesis of uroporphyrinogens from porphobilinogen: mechanism and the nature of the process.
Frydman B; Frydman RB; Valasinas A; Levy ES; Feinstein G
Philos Trans R Soc Lond B Biol Sci; 1976 Feb; 273(924):137-60. PubMed ID: 4834
[TBL] [Abstract][Full Text] [Related]
20. Determination of erythrocyte porphobilinogen deaminase activity using porphobilinogen as substrate.
Hsiao KJ; Lee FY; Wu SJ; Chang WJ
Clin Chim Acta; 1987 Sep; 168(2):257-8. PubMed ID: 3677422
[No Abstract] [Full Text] [Related]
[Next] [New Search]
