Bergonia H, Phillips J
Methods Mol Biol. 2024; 2839:213-223.
PMID: 39008255
DOI: 10.1007/978-1-0716-4043-2_11.
Harder-Viddal C, Roshko R, Stetefeld J
Comput Struct Biotechnol J. 2020; 18:1651-1663.
PMID: 32670505
PMC: 7338781.
DOI: 10.1016/j.csbj.2020.06.025.
Sachar M, Anderson K, Ma X
J Pharmacol Exp Ther. 2015; 356(2):267-75.
PMID: 26588930
PMC: 4727154.
DOI: 10.1124/jpet.115.228130.
Avissar Y, Moberg P
Photosynth Res. 2013; 44(3):221-42.
PMID: 24307093
DOI: 10.1007/BF00048596.
Stetefeld J, Jenny M, Burkhard P
Proc Natl Acad Sci U S A. 2006; 103(37):13688-93.
PMID: 16954186
PMC: 1564225.
DOI: 10.1073/pnas.0600306103.
Oxygen-mediated regulation of porphobilinogen formation in Rhodobacter capsulatus.
Biel A, Canada K, Huang D, Indest K, Sullivan K
J Bacteriol. 2002; 184(6):1685-92.
PMID: 11872720
PMC: 134899.
DOI: 10.1128/JB.184.6.1685-1692.2002.
Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana.
Jones R, Jordan P
Biochem J. 1994; 299 ( Pt 3):895-902.
PMID: 8192681
PMC: 1138105.
DOI: 10.1042/bj2990895.
Porphobilinogen deaminase and uroporphyrinogen III synthase: structure, molecular biology, and mechanism.
Shoolingin-Jordan P
J Bioenerg Biomembr. 1995; 27(2):181-95.
PMID: 7592565
DOI: 10.1007/BF02110033.
Characterization of the porphobilinogen deaminase deficiency in acute intermittent porphyria. Immunologic evidence for heterogeneity of the genetic defect.
Anderson P, Reddy R, Anderson K, Desnick R
J Clin Invest. 1981; 68(1):1-12.
PMID: 7251856
PMC: 370766.
DOI: 10.1172/jci110223.
Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.
Jordan P, Berry A
Biochem J. 1981; 195(1):177-81.
PMID: 6975621
PMC: 1162869.
DOI: 10.1042/bj1950177.
Rare structural variants of human and murine uroporphyrinogen I synthase.
Meisler M, Carter M
Proc Natl Acad Sci U S A. 1980; 77(5):2848-52.
PMID: 6930671
PMC: 349502.
DOI: 10.1073/pnas.77.5.2848.
Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics.
Williams D, Morgan G, McDonald E, BATTERSBY A
Biochem J. 1981; 193(1):301-10.
PMID: 6796041
PMC: 1162603.
DOI: 10.1042/bj1930301.
Characterization of the multiple forms of hydroxymethylbilane synthase from rat spleen.
Williams D
Biochem J. 1984; 217(3):675-83.
PMID: 6712591
PMC: 1153268.
DOI: 10.1042/bj2170675.
Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.
Hart G, Leeper F, BATTERSBY A
Biochem J. 1984; 222(1):93-102.
PMID: 6433896
PMC: 1144148.
DOI: 10.1042/bj2220093.
Purification and properties of uroporphyrinogen III synthase (co-synthetase) from Euglena gracilis.
Hart G, BATTERSBY A
Biochem J. 1985; 232(1):151-60.
PMID: 3936481
PMC: 1152852.
DOI: 10.1042/bj2320151.
Selection by genetic complementation and characterization of the gene coding for the yeast porphobilinogen deaminase.
Gellerfors P, DOUGLAS M
Biochem J. 1986; 240(3):673-7.
PMID: 3548711
PMC: 1147473.
DOI: 10.1042/bj2400673.
Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.
Hart G, ABELL C, BATTERSBY A
Biochem J. 1986; 240(1):273-6.
PMID: 3548707
PMC: 1147405.
DOI: 10.1042/bj2400273.
Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12.
Thomas S, Jordan P
Nucleic Acids Res. 1986; 14(15):6215-26.
PMID: 3529035
PMC: 311632.
DOI: 10.1093/nar/14.15.6215.
A simple rapid purification scheme for hydroxymethylbilane synthase from human erythrocytes.
Smythe E, Williams D
Biochem J. 1988; 251(1):237-41.
PMID: 3390155
PMC: 1148989.
DOI: 10.1042/bj2510237.
Nucleotide sequence for the hemD gene of Escherichia coli encoding uroporphyrinogen III synthase and initial evidence for a hem operon.
Jordan P, Mgbeje B, Thomas S, Alwan A
Biochem J. 1988; 249(2):613-6.
PMID: 3277628
PMC: 1148746.
DOI: 10.1042/bj2490613.
