Prokaryotic heme biosynthesis: multiple pathways to a common essential product
The advent of heme during evolution allowed organisms possessing this compound to
safely and efficiently carry out a variety of chemical reactions that otherwise were difficult or …
safely and efficiently carry out a variety of chemical reactions that otherwise were difficult or …
Pyrrole N–H anion complexes
GI Vargas-Zúñiga, JL Sessler - Coordination chemistry reviews, 2017 - Elsevier
Synthetic pyrrole-based anion receptors date back to the 1990s. They have been
extensively developed in the context of macrocyclic systems such as expanded porphyrins …
extensively developed in the context of macrocyclic systems such as expanded porphyrins …
Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site
GV Louie, PD Brownlie, R Lambert, JB Cooper… - Nature, 1992 - nature.com
The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic
pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 Å resolution. Two of the …
pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 Å resolution. Two of the …
ALAD Inhibition by porphobilinogen rationalizes the accumulation of δ-aminolevulinate in acute porphyrias
I San Juan, T Pereira-Ortuzar, X Cendoya, A Laín… - Biochemistry, 2022 - ACS Publications
Patients with major forms of acute hepatic porphyria present acute neurological attacks with
overproduction of porphobilinogen (PBG) and δ-aminolevulinic acid (ALA). Even if ALA is …
overproduction of porphobilinogen (PBG) and δ-aminolevulinic acid (ALA). Even if ALA is …
The three‐dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76‐Å resolution
GV Louie, PD Brownlie, R Lambert… - Proteins: Structure …, 1996 - Wiley Online Library
Porphobilinogen deaminase (PBGD) catalyses the polymerization of four molecules of
porphobilinogen to form the 1‐hydroxymethylbilane, preuroporphyrinogen, a key …
porphobilinogen to form the 1‐hydroxymethylbilane, preuroporphyrinogen, a key …
Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana.
RM Jones, PM Jordan - Biochemical journal, 1994 - ncbi.nlm.nih.gov
Abstract 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 …
(16,000-fold) from the plant Arabidopsis thaliana in yields of 8%. The deaminase is a …
Determination of the structure of selenomethionine-labelled hydroxymethylbilane synthase in its active form by multi-wavelength anomalous dispersion
A Hädener, PK Matzinger, AR Battersby… - … Section D: Biological …, 1999 - journals.iucr.org
The enzyme hydroxymethylbilane synthase (HMBS, EC 4.3. 1.8) catalyzes the conversion of
porphobilinogen into hydroxymethylbilane, a key intermediate for the biosynthesis of heme …
porphobilinogen into hydroxymethylbilane, a key intermediate for the biosynthesis of heme …
Advances in Anion Sensing Using Dipyrromethane‐Based Compounds
S Acharya, L Nayak, S Routray, R Satapathy - ChemistrySelect, 2024 - Wiley Online Library
Anion sensing plays a crucial role in areas ranging from medical diagnostics to
environmental monitoring. Dipyrromethane‐based compounds offer a versatile platform for …
environmental monitoring. Dipyrromethane‐based compounds offer a versatile platform for …
Purification, characterization, crystallisation and X‐ray analysis of selenomethionine‐labelled hydroxymethylbilane synthase from Escherichia coli
A Hädener, PK Matzinger… - European journal of …, 1993 - Wiley Online Library
Hydroxymethylbilane synthase (HMBS) catalyses the conversion of porphobilinogen into
hydroxymethylbilane, a linear tetrapyrrolic intermediate in the biosynthesis of haems …
hydroxymethylbilane, a linear tetrapyrrolic intermediate in the biosynthesis of haems …
Reconstitution of the Holoenzyme Form of Escherichia coli Porphobilinogen Deaminase from Apoenzyme with Porphobilinogen and Preuroporphyrinogen: A Study …
SJ Awan, G Siligardi, PM Shoolingin-Jordan… - Biochemistry, 1997 - ACS Publications
Porphobilinogen deaminase (PBG-D), an early enzyme of the tetrapyrrole biosynthetic
pathway, catalyzes the formation of a tetrapyrrole chain, preuroporphyrinogen, from four …
pathway, catalyzes the formation of a tetrapyrrole chain, preuroporphyrinogen, from four …