Results 111 to 120 of about 118,565,731 (151)

Protein-Protein Interactions in the Mammalian Heme Degradation Pathway: Heme Oxygenase-2, Cytochrome P450 Reductase and Biliverdin Reductase. [PDF]

open access: yes, 2014
Heme oxygenase (HO) catalyzes the rate-limiting step in the degradation of heme to biliverdin, CO and Fe, and requires electrons delivered from NADPH via cytochrome P450 reductase (CPR).
Spencer, Andrea L. M.
core  

Biliverdin Reductase of Guinea Pig Liver

open access: yesJournal of Biological Chemistry, 1965
J W, Singleton, L, Laster
openaire   +2 more sources

Preparation of Bilirubin Through the Biotransformation of Biliverdin Using Whole Cells of Recombinant Yeast

open access: yes
Bilirubin is a key component in the preparation of two traditional Chinese medicines: Calculus bovis sativus and Calculus bovis artifactus. Currently, industrial-scale production of bilirubin is limited to extraction from pig bile in a very low yield and
Yanchao Han   +4 more
core   +1 more source

Kinetic studies on biliverdin-IXalpha reductase

open access: yes, 2019
The species distribution of biliverdin-IXa reductase (BVR-A) has been reinvestigated. It appears increasingly likely that birds and amphibia have the potential to express an active biliverdin-IXa reductase. The full length cDNAs encoding human, Danio rerio, murine, and Xenopus BVR-A were successfully amplified and cloned into various expression vectors.
openaire   +1 more source

Biliverdin Reductase Isozymes in Metabolism [PDF]

open access: yesTrends in Endocrinology and Metabolism, 2015
The biliverdin reductase (BVR) isozymes BVRA and BVRB are cell surface membrane receptors with pleiotropic functions. This review compares, for the first time, the structural and functional differences between the isozymes. They reduce biliverdin, a byproduct of heme catabolism, to bilirubin, display kinase activity, and BVRA, but not BVRB, can act as ...
David E Stec, Kezia John, Terry D Hinds
exaly   +4 more sources

Biliverdin Inhibits Activation of NF-κB: Reversal of Inhibition by Human Biliverdin Reductase [PDF]

open access: yesInternational Journal of Cancer, 2007
AbstracthBVR functions in the cell as a reductase and as a kinase. In the first capacity, it reduces biliverdin, the product of HO activity, to the effective intracellular antioxidant, bilirubin; as a dual‐specificity kinase (S/T/Y) it activates the MAPK and IGF/IRK receptor signal transduction pathways. NF‐κB and the MAPK pathway are activated by ROS,
Peter E M Gibbs, Mahin D Maines
exaly   +3 more sources

The Specificity of Biliverdin Reductase: The Reduction of Biliverdin XIII Isomers

BBA - Proteins and Proteomics, 1984
The substrate specificity of the different molecular forms of biliverdin reductase (bilirubin:NAD(P)+ oxidoreductase, EC 1.3.1.24) using biliverdin XIII alpha, XIII beta and XIII gamma was examined. It was found that molecular form 1 (the major form in normal rat liver) reduced biliverdin XIII alpha at a much higher rate than the other two isomers ...
J Awruch   +2 more
exaly   +2 more sources

Overexpression of Biliverdin Reductase Enhances Resistance to Chemotherapeutics

Cancer Letters, 2011
Biliverdin reductase (BVR) converts biliverdin to bilirubin. Additionally, acting as a transcription factor and possessing a capacity of a serine/threonine kinase, it may modulate signaling pathways. In order to gain better understanding of BVR functions, we used genetically modified line of mouse fibroblasts with reversible overexpression of BVR ...
Józef Dulak   +2 more
exaly   +3 more sources

Biliverdin Reductase: Substrate Specificity and Kinetics

BBA - Proteins and Proteomics, 1987
The substrate specificity of the different forms of rat liver biliverdin reductase was examined using synthetic biliverdins. Biliverdins carrying methyl, ethyl and one propionate residue in their structure were not substrates of biliverdin reductase. Biliverdins with one propionate and one acetate residue or with two acetate residues were not reduced ...
J Awruch   +2 more
exaly   +3 more sources

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