Results 131 to 140 of about 5,120 (161)

Therapeutic potential of 5-aminolevulinic acid in metabolic disorders: Current insights and future directions. [PDF]

iScience
Kuryata O, Akimov O, Riabushko M, Kostenko H, Kostenko V, Mishchenko A, Nazarenko S, Solovyova N, Kostenko V.   +8 more
europepmc   +1 more source

Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12

Gene, 1993
Among the photoresistant revertants of the visA-deleted (hemH-deleted) strain of Escherichia coli K-12, three mutants defective in the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) were identified. Using one of the mutants, we cloned and sequenced the hemE of E. coli. We found an open reading frame of 353 codons, which encoded a predicted
K, Nishimura, T, Nakayashiki, H, Inokuchi   +2 more
semanticscholar   +5 more sources

Density-Functional Study of Mechanisms for the Cofactor-Free Decarboxylation Performed by Uroporphyrinogen III Decarboxylase

The Journal of Physical Chemistry B, 2005
Uroporphyrinogen III decarboxylase catalyzes the fifth step in heme biosynthesis: the elimination of carboxyl groups from the four acetate side chains of uroporphyrinogen III to yield coproporphyrinogen III. The enzyme acts by successively protonating each of the four pyrrole rings present in the substrate, thereby allowing decarboxylation of their ...
Pedro J, Silva, Maria João, Ramos
semanticscholar   +4 more sources

Random decarboxylation of uroporphyrinogen III by human hepatic uroporphyrinogen decarboxylase

Journal of Chromatography B: Biomedical Sciences and Applications, 1991
The type III heptacarboxylic porphyrinogens derived from enzymic decarboxylation of an acetic acid substituent on uroporphyrinogen III to a methyl group by human hepatic uroporphyrinogen decarboxylase has been analysed by reversed-phase high-performance liquid chromatography with electrochemical detection.
J L, Luo, C K, Lim
semanticscholar   +4 more sources

Tobacco uroporphyrinogen-III decarboxylase: characterization, crystallization and preliminary X-ray analysis

Acta Crystallographica Section D Biological Crystallography, 2001
Uroporphyrinogen-III decarboxylase from Nicotiana tabacum is a plastidial enzyme involved in the biosynthesis of chlorophyll and haem. Sedimentation equilibrium with protein producing diffracting crystals clearly indicates that the enzyme is a homodimer under similar ionic strength conditions to those found in the chloroplast stroma.
B M, Martins, B, Grimm, H P, Mock, G, Richter, R, Huber, A, Messerschmidt   +5 more
semanticscholar   +4 more sources

The first branching point in porphyrin biosynthesis: A systematic docking, molecular dynamics and quantum mechanical/molecular mechanical study of substrate binding and mechanism of uroporphyrinogen‐III decarboxylase

Journal of Computational Chemistry, 2010
AbstractIn humans, uroporphyrinogen decarboxylase is intimately involved in the synthesis of heme, where the decarboxylation of the uroporphyrinogen‐III occurs in a single catalytic site. Several variants of the mechanistic proposal exist; however, the exact mechanism is still debated.
Eric A C, Bushnell, Edvin, Erdtman, Jorge, Llano, Leif A, Eriksson, James W, Gauld   +4 more
semanticscholar   +4 more sources

Localisation of Plasmodium falciparum uroporphyrinogen III decarboxylase of the heme-biosynthetic pathway in the apicoplast and characterisation of its catalytic properties

International Journal for Parasitology, 2009
Uroporphyrinogen decarboxylase (UROD) is a key enzyme in the heme-biosynthetic pathway and in Plasmodium falciparum it occupies a strategic position in the proposed hybrid pathway for heme biosynthesis involving shuttling of intermediates between different subcellular compartments in the parasite.
Nagaraja, Viswanathan Arun, Arumugam, Rajavel, Chandra, Nagasuma R, Prasad, Dasari, Rangarajan, Pundi N, Padmanaban, Govindarajan   +5 more
semanticscholar   +4 more sources