Structural basis of pyrrole polymerization in human porphobilinogen deaminase [PDF]
Biochimica Et Biophysica Acta - General Subjects, 2018 Human porphobilinogen deaminase (PBGD), the third enzyme in the heme pathway, catalyzes four times a single reaction to convert porphobilinogen into hydroxymethylbilane. Remarkably, PBGD employs a single active site during the process, with a distinct yet chemically equivalent bond formed each time.
Pietro Roversi +2 more
exaly +9 more sources
PORPHOBILINOGEN DEAMINASE Deficiency Alters Vegetative and Reproductive Development and Causes Lesions in Arabidopsis [PDF]
PLoS ONE, 2013 The Arabidopsis rugosa1 (rug1) mutant has irregularly shaped leaves and reduced growth. In the absence of pathogens, leaves of rug1 plants have spontaneous lesions reminiscent of those seen in lesion-mimic mutants; rug1 plants also express cytological ...
Raquel Sarmiento-Mañús +2 more
exaly +6 more sources
Isolation and Characterization of SPOTTED LEAF42 Encoding a Porphobilinogen Deaminase in Rice [PDF]
Plants, 2023 The formation and development of chloroplasts play a vital role in the breeding of high-yield rice (Oryza sativa L.). Porphobilinogen deaminases (PBGDs) act in the early stage of chlorophyll and heme biosynthesis.
Lin Liu +11 more
doaj +5 more sources
AbhemC encoding porphobilinogen deaminase plays an important role in chlorophyll biosynthesis and function in albino Ananas comosus var. bracteatus leaves [PDF]
PeerJ, 2021 Background The chimeric leaves of Ananas comosus var. bracteatus are composed of normal green parts (Grs) and albino white parts (Whs). Although the underlying mechanism of albinism in A. comosus var.
Yanbin Xue +9 more
doaj +5 more sources
Enigmatic Evolutionary History of Porphobilinogen Deaminase in Eukaryotic Phototrophs [PDF]
Biology, 2021 In most eukaryotic phototrophs, the entire heme synthesis is localized to the plastid, and enzymes of cyanobacterial origin dominate the pathway.
Miroslav Oborník
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Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilane. [PDF]
PLoS Computational Biology, 2014 Porphobilinogen deaminase (PBGD) catalyzes the formation of 1-hydroxymethylbilane (HMB), a crucial intermediate in tetrapyrrole biosynthesis, through a step-wise polymerization of four molecules of porphobilinogen (PBG), using a unique dipyrromethane ...
Navneet Bung +3 more
doaj +5 more sources
Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism [PDF]
iScience, 2021 Summary: Porphobilinogen deaminase (PBGD), the third enzyme in the heme biosynthesis, catalyzes the sequential coupling of four porphobilinogen (PBG) molecules into a heme precursor. Mutations in PBGD are associated with acute intermittent porphyria (AIP)
Helene J. Bustad +6 more
doaj +3 more sources
The crystal structures of the enzyme hydroxymethylbilane synthase, also known as porphobilinogen deaminase. [PDF]
Acta Crystallogr F Struct Biol Commun, 2021 Thirty years of crystal structures of the enzyme hydroxymethylbilane synthase are surveyed in this topical review. These crystal structures aim at the elucidation of the structural basis of the complex reaction mechanism involving the formation of ...
Helliwell JR.
europepmc +4 more sources
Host Porphobilinogen Deaminase Deficiency Confers Malaria Resistance in Plasmodium chabaudi but Not in Plasmodium berghei or Plasmodium falciparum During Intraerythrocytic Growth [PDF]
Frontiers in Cellular and Infection Microbiology, 2020 An important component in host resistance to malaria infection are inherited mutations that give rise to abnormalities and deficiencies in erythrocyte proteins and enzymes.
Cilly Bernardette Schnider +13 more
doaj +3 more sources
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana. [PDF]
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 Roberts A +8 more
europepmc +3 more sources