Results 171 to 180 of about 4,609 (210)

Yeast Porphobilinogen Deaminase also Forms Enzyme-Pyrrole Intermediates

Enzyme and Protein, 1994
The enzyme porphobilinogen deaminase (PBG deaminase, EC 4.3.1.8) catalyzes the condensation of four molecules of PBG to give the linear tetrapyrrol, hydroxymethylbilane. It has been shown that this enzyme forms stable mono-, di-, tri- and tetrapyrrole-enzyme covalent complexes.
S, Correa Garcia, M V, Rossetti, M, Bermudez Moretti, A M, Batlle   +3 more
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Erythrocyte Porphobilinogen Deaminase Activity in Lives Disease

Gastroenterology, 1987
The activities of erythrocyte porphobilinogen deaminase were studied in patients with various liver diseases and in control groups. The lowest enzyme activities were found in patients with acute intermittent porphyria, and the highest ones in those with increased hemopoietic activity.
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Schizophrenia and porphobilinogen deaminase gene polymorphisms: an association study

Schizophrenia Research, 1992
A genetic case-control study was conducted in a group of patients with schizophrenia (n = 67; DSM-III) and psychiatrically normal controls matched for ethnicity (n = 84), living in the same geographical area. Using three different DNA polymorphisms of the gene encoding porphobilinogen deaminase (PBGD), a candidate gene for schizophrenia, an association
V L, Nimgaonkar, R, Ganguli, S S, Washington, A, Chakravarti   +3 more
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Structural studies on porphobilinogen deaminase.

Ciba Foundation symposium, 1995
The X-ray crystallographic analysis of porphobilinogen deaminase (hydroxymethylbilane synthase, EC 4.3.1.8) shows the polypeptide chain folded into three domains, (1) N-terminal, (2) central and (3) C-terminal, of approximately equal size. Domains 1 and 2 have a similar overall topology, a modified doubly wound parallel beta-sheet.
R, Lambert, P D, Brownlie, S C, Woodcock, G V, Louie, J C, Cooper, M J, Warren, P M, Jordan, T L, Blundell, S P, Wood   +8 more
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Characterization and Regulation of the Nonerythroid Porphobilinogen Deaminase Promoter

Biochemical and Biophysical Research Communications, 1997
The non-erythroid porphobilinogen deaminase (E.C. 4.3.1.8) promoter was investigated according to sequence changes and transcriptional activity. The minimal promoter sequence required for maximal transcription, was localized by deletion mapping to -243 to -115 relative to the translational start site.
G, Lundin, M, Anvret
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Purification and properties of porphobilinogen deaminase from wheat germ

Archives of Biochemistry and Biophysics, 1970
Abstract Porphobilinogen deaminase from wheat germ was purified about 1000-fold. A series of DEAE-cellulose fractionations gave varying yields of uroporphyrin formation. The properties of the purified wheat germ enzyme were studied and compared with PBG deaminases from other origins such as Swiss chard leaves, human erythrocytes, and Rhodospirillum ...
R B, Frydman, B, Frydman
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Frequency of low erythrocyte porphobilinogen deaminase activity in Finland*

Journal of Internal Medicine, 1992
Abstract. The frequency of low erythrocyte porphobilinogen deaminase (PBGD) activity was investigated in 2234 blood donors and in 30 patients with acute intermittent porphyria. The mean enzyme activities (± SD) were 3.38 ± 0.58 U and 1.82 ± 0.41 U, respectively.
P, Mustajoki, R, Kauppinen, L, Lannfelt, L, Lilius, J, Koistinen   +4 more
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Tissue‐specific expression of porphobilinogen deaminase

European Journal of Biochemistry, 1987
Porphobilinogen deaminase (hydroxymethylbilane synthase; EC 4.3.1.8), the third enzyme of the heme biosynthetic pathway, catalyzes the stepwise condensation of four porphobilinogen units to yield hydroxymethylbilan, which is in turn converted to uroporphyrinogen III by cosynthetase.
B, Grandchamp, H, De Verneuil, C, Beaumont, S, Chretien, O, Walter, Y, Nordmann   +5 more
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Studies on cow liver porphobilinogen deaminase.

Acta physiologica latino americana, 1978
Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single badn on starch and polycrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B 10-Gel P-100, gave values of 40 000 +/- 4 000.
H A, Sancovich, A M, Ferramola, A M, del C Batlle, A, Kivilevich, M, Grinstein   +4 more
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Human erythroid porphobilinogen deaminase exists in 2 splice variants

Blood, 2001
AbstractHuman porphobilinogen deaminase (PBGD) is, reportedly, encoded by 2 distinct messenger RNAs (mRNAs) transcribing from a single gene. The ubiquitous form of the PBGD gene product is often used as an endogenous reference in gene expression studies because it is pseudogene free and has minimal transcriptional variability among tissues.
A N, Gubin, J L, Miller
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