Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Peter M. Jordan"'
Autor:
Peter M. Jordan, R M Jones
Publikováno v:
Biochemical Journal. 299:895-902
Porphobilinogen deaminase (EC 4.3.1.8) has been purified to homogeneity (16,000-fold) from the plant Arabidopsis thaliana in yields of 8%. The deaminase is a monomer of M(r) 35,000, as shown by SDS/PAGE, and 31,000, using gel-filtration chromatograph
Publikováno v:
Tetrahedron Letters. 34:1177-1180
Glutamate 1-semialdehyde is shown to exist in a cyclic form, 5-amino-6-hydroxy-3,4,5,6-tetrahydropyran-2-one (HAT), which explains its unexpectedly high stability for an α-aminoaldehyde. It is proposed that the cyclic form is the actual intermediate
Autor:
Jonathan B. Spencer, Peter M. Jordan
Publikováno v:
Biochemical Society Transactions. 21:222-228
Autor:
Jonathan B. Spencer, Peter M. Jordan
Publikováno v:
Tetrahedron. 47:6015-6028
Chiral malonates, (R)-[1-13C;2-2H]malonate and (S)-[1-13C;2-2H]malonate, were synthesised and characterised as malonyl-CoA derivatives with yeast fatty acid synthase using mass spectrometric analysis of the palmitic acid produced. The chiral malonate
Autor:
Harry A. Dailey, Peter M. Jordan
Publikováno v:
Molecular Aspects of Medicine. 11:21-37
Autor:
Peter M. Jordan
Publikováno v:
Ciba Foundation Symposium 180-The Biosynthesis of the Tetrapyrrole Pigments
The biosynthesis of the uroporphyrinogen III macrocycle from porphobilinogen requires the sequential participation of two enzymes--porphobilinogen deaminase (1-hydroxymethylbilane synthase, EC 4.3.1.8) and uroporphyrinogen III synthase (cosynthase, E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5fa2cc1ef5f7ffffc7b534cb76534d62
https://doi.org/10.1002/9780470514535.ch5
https://doi.org/10.1002/9780470514535.ch5
Autor:
Martin J. Warren, Gordon V. Louie, Sarah C. Woodcock, Peter M. Jordan, Paul D. Brownlie, Tom L. Blundell, Steve P. Wood, Richard Lambert, Cooper Jc
Publikováno v:
Ciba Foundation Symposium 180-The Biosynthesis of the Tetrapyrrole Pigments
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::820d0f41551c4f54d09804ec459239fe
https://doi.org/10.1002/9780470514535.ch6
https://doi.org/10.1002/9780470514535.ch6
Autor:
Paul D. Brownlie, B I A Mgbeje, Jonathan B. Cooper, Richard Lambert, Peter M. Jordan, S.P. Wood, Gordon V. Louie, Martin J. Warren, Tom L. Blundell
Publikováno v:
Journal of Molecular Biology. 224:269-271
Porphobilinogen deaminase, the polymerase that catalyses the synthesis of preuroporphyrinogen, the linear tetrapyrrole precursor of uroporphyrinogen III, has been crystallized from sodium acetate buffer with polyethylene glycol 6000 as precipitant. T
Publikováno v:
Planta. 199(4)
A recombinant plasmid, pArab8, harbouring the cDNA encoding the mature form of the tetrapyrrole synthesis enzyme porphobilinogen deaminase (EC 4.3.1.8; also known as hydroxymethylbilane synthase) from Arabidopsis thaliana (L.) Heynh. has been constru
Publikováno v:
Molecular medicine today. 1(5)
Acute intermittent porphyria is an inherited disease of haem biosynthesis that results from mutation of the gene for the enzyme porphobilinogen deaminase. Many different mutations have been located throughout the gene. The three-dimensional structure