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Activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions.
Franklin E
,
Browne S
,
Hayes J
,
Boland C
,
Dunne A
,
Elliot G
,
Mantle TJ
.
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The effect of pH on the initial-rate kinetic behaviour of BVR-A (biliverdin-IXalpha reductase) exhibits an alkaline optimum with NADPH as cofactor, but a neutral optimum with NADH as cofactor. This has been described as dual cofactor and dual pH dependent behaviour; however, no mechanism has been described to explain this phenomenon. We present evidence that the apparent peak of activity observed at neutral pH with phosphate buffer and NADH as cofactor is an anion-dependent activation, where inorganic phosphate apparently mimics the role played by the 2'-phosphate of NADPH in stabilizing the interaction between NADH and the enzyme. The enzymes from mouse, rat and human all exhibit this behaviour. This behaviour is not seen with BVR-A from Xenopus tropicalis or the ancient cyanobacterial enzyme from Synechocystis PCC 6803, which, in addition to being refractory to activation by inorganic phosphate, are also differentiated by an acid pH optimum with both nicotinamide nucleotides.
Baranano,
Biliverdin reductase: a major physiologic cytoprotectant.
2002, Pubmed
Baranano,
Biliverdin reductase: a major physiologic cytoprotectant.
2002,
Pubmed
Berman,
The Protein Data Bank.
2000,
Pubmed
Christensen,
Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.
2005,
Pubmed
Converso,
HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism.
2006,
Pubmed
Cunningham,
Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites.
2000,
Pubmed
Desmoulin,
Phosphorus-31 nuclear-magnetic-resonance study of phosphorylated metabolites compartmentation, intracellular pH and phosphorylation state during normoxia, hypoxia and ethanol perfusion, in the perfused rat liver.
1987,
Pubmed
Elliott,
Purification and properties of salmon liver biliverdin reductase.
1995,
Pubmed
Ennis,
Cloning and overexpression of rat kidney biliverdin IX alpha reductase as a fusion protein with glutathione S-transferase: stereochemistry of NADH oxidation and evidence that the presence of the glutathione S-transferase domain does not effect BVR-A activity.
1997,
Pubmed
Fakhrai,
Expression and characterization of a cDNA for rat kidney biliverdin reductase. Evidence suggesting the liver and kidney enzymes are the same transcript product.
1992,
Pubmed
Fisher,
Modification of a PCR-based site-directed mutagenesis method.
1997,
Pubmed
Fondevila,
Biliverdin therapy protects rat livers from ischemia and reperfusion injury.
2004,
Pubmed
Foresti,
Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults.
2004,
Pubmed
Kapitulnik,
Bilirubin: an endogenous product of heme degradation with both cytotoxic and cytoprotective properties.
2004,
Pubmed
Kikuchi,
Crystal structure of rat biliverdin reductase.
2001,
Pubmed
Kutty,
Purification and characterization of biliverdin reductase from rat liver.
1981,
Pubmed
Lennon,
The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression.
1996,
Pubmed
Llorente,
Regulation of liver pyruvate kinase and the phosphoenolpyruvate crossroads.
1970,
Pubmed
Maines,
Purification and characterization of human biliverdin reductase.
1993,
Pubmed
Maines,
Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes.
1996,
Pubmed
Marco,
Oxaloacetate metabolic crossroads in liver. Enzyme compartmentation and regulation of gluconeogenesis.
1974,
Pubmed
Nakao,
Protection against ischemia/reperfusion injury in cardiac and renal transplantation with carbon monoxide, biliverdin and both.
2005,
Pubmed
Nakao,
Biliverdin protects the functional integrity of a transplanted syngeneic small bowel.
2004,
Pubmed
Noguchi,
Purification and properties of biliverdin reductases from pig spleen and rat liver.
1979,
Pubmed
Phillips,
Some kinetic and physical properties of biliverdin reductase.
1981,
Pubmed
Phillips,
On the possible role of biliverdin stimulation of cyclic AMP levels as a trigger for liver regeneration in the rat.
1984,
Pubmed
Rigney,
Some physical and immunological properties of ox kidney biliverdin reductase.
1988,
Pubmed
Rigney,
The kinetics of ox kidney biliverdin reductase in the pre-steady state. Evidence that the dissociation of bilirubin is the rate-determining step.
1989,
Pubmed
Ryter,
Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications.
2006,
Pubmed
Sarady-Andrews,
Biliverdin administration protects against endotoxin-induced acute lung injury in rats.
2005,
Pubmed
Schluchter,
Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis.
1997,
Pubmed
Whitby,
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
2002,
Pubmed
Wu,
Stability of NADPH: effect of various factors on the kinetics of degradation.
1986,
Pubmed
Yamaguchi,
Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization.
1994,
Pubmed
Yamashita,
Biliverdin, a natural product of heme catabolism, induces tolerance to cardiac allografts.
2004,
Pubmed