Results 221 to 230 of about 732,679 (273)

A primer on heme biosynthesis

Biological Chemistry, 2022
Heme (protoheme IX) is an essential cofactor for a large variety of proteins whose functions vary from one electron reactions to binding gases. While not ubiquitous, heme is found in the great majority of known life forms.
H. Dailey, Amy E. Medlock
semanticscholar   +3 more sources

Heme biosynthesis and its regulation: towards understanding and improvement of heme biosynthesis in filamentous fungi [PDF]

Applied Microbiology and Biotechnology, 2011
Heme biosynthesis in fungal host strains has acquired considerable interest in relation to the production of secreted heme-containing peroxidases.
Arthur F J Ram, Peter J Punt, Cees A M J J van den Hondel   +2 more
exaly   +6 more sources

High-level Secretory Production of Leghemoglobin in Pichia pastoris through Enhanced Globin Expression and Heme Biosynthesis.

Bioresource Technology, 2022
Soy leghemoglobin is a key food additive that imparts meaty flavor and color to meat analogs. Here, a Pichia pastoris strain capable of high-yield secretory production of functional leghemoglobin was developed through gene dosage optimization and heme ...
Youran Shao, Chang-Lu Xue, Wen-quan Liu, Siqi Zuo, Peilian Wei, Lei Huang, Jia-Zhang Lian, Zhi-Nan Xu   +7 more
semanticscholar   +1 more source

Heme biosynthesis in the heart

Biochemical Pharmacology, 1982
The rates of biosynthesis of heme a and heme b in hearts of fed and fasted rats were measured using an isolated heart perfusion system. delta-Aminolevulinic acid synthetase activity was decreased in hearts of fasted rats to about 30% of values in hearts obtained from fed rats.
R, Sedman, G, Ingall, G, Rios, T R, Tephly   +3 more
openaire   +2 more sources

The biochemistry of heme biosynthesis

Archives of Biochemistry and Biophysics, 2008
Heme is an integral part of proteins involved in multiple electron transport chains for energy recovery found in almost all forms of life. Moreover, heme is a cofactor of enzymes including catalases, peroxidases, cytochromes of the P(450) class and part of sensor molecules.
Ilka U, Heinemann, Martina, Jahn, Dieter, Jahn   +2 more
openaire   +2 more sources

Biosynthesis of Hemes

EcoSal Plus, 2007
This review is concerned specifically with the structures and biosynthesis of hemes in E. coli and serovar Typhimurium. However, inasmuch as all tetrapyrroles share a common biosynthetic pathway, much of the material covered here is applicable to tetrapyrrole biosynthesis in other organisms.
openaire   +2 more sources

The Biosynthesis of Heme O and Heme A Is Not Regulated by Copper

Biochemistry, 2005
Heme A is an obligatory cofactor in all eukaryotic and many prokaryotic cytochrome c oxidase (CcO) enzymes. Despite its obvious importance to CcO and the electron transport pathway, essentially nothing is known concerning the regulation of heme A. Because CcO is the only natural target for heme A and copper is also required for CcO activity, it was ...
M Scott, Morrison, Julia A, Cricco, Eric L, Hegg   +2 more
openaire   +2 more sources

IDH1 mutation contributes to myeloid dysplasia in mice by disturbing heme biosynthesis and erythropoiesis.

Blood, 2020
Isocitrate dehydrogenase (IDH) mutations are common genetic alterations in myeloid disorders, including acute myeloid leukemia (AML) and myelodysplastic syndrome (MDS).
Yu Gu, Risheng Yang, Ying Yang, Yuanlin Zhao, A. Wakeham, Wanda Li, A. Tseng, J. Leca, T. Berger, M. Saunders, J. Fortin, Xing Gao, Yuan Yuan, Li-Ming Xiao, Feng Zhang, Lijun Zhang, Guang-Xun Gao, Wen-Jing Zhou, Zhe Wang, T. Mak, Jing Ye   +20 more
semanticscholar   +1 more source

Bilirubin Inhibition of Heme Biosynthesis

Science, 1959
The conversion of protoporphyrin and iron to heme is catalyzed by a soluble enzyme prepared from rat liver. This reaction is inhibited by bilirubin, and initial kinetic studies suggest that the inhibition is due in part to a competition between protoporphyrin and the bile pigment. Implications of this finding in hyperbilirubinemia are mentioned.
R F, LABBE, M R, ZASKE, R A, ALDRICH
openaire   +2 more sources

Structure and function of enzymes in heme biosynthesis [PDF]

Protein Science, 2010
AbstractTetrapyrroles like hemes, chlorophylls, and cobalamin are complex macrocycles which play essential roles in almost all living organisms. Heme serves as prosthetic group of many proteins involved in fundamental biological processes like respiration, photosynthesis, and the metabolism and transport of oxygen.
Gunhild Layer, Dieter Jahn, Dirk Heinz
exaly   +4 more sources