Results 31 to 40 of about 42,175 (244)

Sedimentary Cobalt Protoporphyrin as a Potential Precursor of Prosthetic Heme Group for Bacteria Inhabiting Fossil Organic Matter-Rich Shale Rock

open access: yesBiomolecules, 2021
This study hypothesizes that bacteria inhabiting shale rock affect the content of the sedimentary cobalt protoporphyrin present in it and can use it as a precursor for heme synthesis.
Robert Stasiuk, Renata Matlakowska
doaj   +1 more source

Deconvoluting heme biosynthesis to target blood-stage malaria parasites

open access: yeseLife, 2015
Heme metabolism is central to blood-stage infection by the malaria parasite Plasmodium falciparum. Parasites retain a heme biosynthesis pathway but do not require its activity during infection of heme-rich erythrocytes, where they can scavenge host heme ...
Paul A Sigala   +3 more
doaj   +1 more source

Biosynthesis of High‐Active Hemoproteins by the Efficient Heme‐Supply Pichia Pastoris Chassis

open access: yesAdvanced Science, 2023
Microbial synthesis of valuable hemoproteins has become a popular research topic, and Pichia pastoris is a versatile platform for the industrial production of recombinant proteins.
Fei Yu   +6 more
doaj   +1 more source

Heme biosensor-guided in vivo pathway optimization and directed evolution for efficient biosynthesis of heme

open access: yesBiotechnology for Biofuels and Bioproducts, 2023
Background Heme has attracted much attention because of its wide applications in medicine and food. The products of genes hemBCDEFY convert 5-aminolevulinic acid to protoporphyrin IX (PPIX; the immediate precursor of heme); protoporphyrin ferrochelatase (
Jian Zhang   +7 more
doaj   +1 more source

Fine-Tuning of hemB Using CRISPRi for Increasing 5-Aminolevulinic Acid Production in Escherichia coli

open access: yesFrontiers in Microbiology, 2019
5-aminolevulinic acid (5-ALA) is an important metabolic intermediate in the biosynthesis of heme and has been broadly applied in medicine, agriculture, and organic synthesis.
Tianyuan Su   +6 more
doaj   +1 more source

Coordination of metal center biogenesis in human cytochrome c oxidase

open access: yesNature Communications, 2022
Mitochondrial cytochrome c oxidase is a heme aa3-copper oxygen reductase. Here, authors report that metal center-specific metallochaperones form dynamic assemblies to control heme a biosynthesis and coordinate copper transfer to the copper sites.
Eva Nývltová   +4 more
doaj   +1 more source

Circadian Genes Expression Patterns in Disorders Due to Enzyme Deficiencies in the Heme Biosynthetic Pathway

open access: yesBiomedicines, 2022
Heme is a member of the porphyrins family of cyclic tetrapyrroles and influences various cell processes and signalling pathways. Enzyme deficiencies in the heme biosynthetic pathway provoke rare human inherited metabolic diseases called porphyrias ...
Maria Savino   +11 more
doaj   +1 more source

Generation and characterization of human U-2 OS cell lines with the CRISPR/Cas9-edited protoporphyrinogen oxidase IX gene

open access: yesScientific Reports, 2022
In humans, disruptions in the heme biosynthetic pathway are associated with various types of porphyrias, including variegate porphyria that results from the decreased activity of protoporphyrinogen oxidase IX (PPO; E.C.1.3.3.4), the enzyme catalyzing the
Zora Novakova   +11 more
doaj   +1 more source

Microbial Synthesis of Heme b: Biosynthetic Pathways, Current Strategies, Detection, and Future Prospects

open access: yesMolecules, 2023
Heme b, which is characterized by a ferrous ion and a porphyrin macrocycle, acts as a prosthetic group for many enzymes and contributes to various physiological processes. Consequently, it has wide applications in medicine, food, chemical production, and
Qiuyu Yang   +4 more
doaj   +1 more source

Heme A biosynthesis

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2012
Respiration in plants, most animals and many aerobic microbes is dependent on heme A. This is a highly specialized type of heme found as prosthetic group in cytochrome a-containing respiratory oxidases. Heme A differs structurally from heme B (protoheme IX) by the presence of a hydroxyethylfarnesyl group instead of a vinyl side group at the C2 position
openaire   +2 more sources

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