Biliverdin reductase: substrate specificity and kinetics

Frydman, Rosalía B.; Tomaro, Marı́a L.; Rosenfeld, Jorge; Awruch, Josefina; Sambrotta, Luis; Valasinas, Aldonia; Frydman, Benjamiǹ

doi:10.1016/0167-4838(87)90197-x

Cited by 21 publications

(10 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Biliverdin reductase has been known for many decades as the second enzyme in the heme degradation pathway necessary for conversion of BV to BR (Frydman et al, 1987; Bell and Maines, 1988) which serves as both a radical scavenger (Stocker et al, 1987), but is also critical in lipid emulsion during digestion. There are two isoforms of BVR.…”

Section: Bvr-identification and Characterizationmentioning

confidence: 99%

Go Green: The Anti-Inflammatory Effects of Biliverdin Reductase

Węgiel¹,

Otterbein²

2012

Front. Pharmacol.

118

View full text Add to dashboard Cite

Biliverdin (BV) has emerged as a cytoprotective and important anti-inflammatory molecule. Conversion of BV to bilirubin (BR) is catalyzed by biliverdin reductase (BVR) and is required for the downstream signaling and nuclear localization of BVR. Recent data by others and us make clear that BVR is a critical regulator of innate immune responses resulting from acute insult and injury and moreover, that a lack of BVR results in an enhanced proinflammatory phenotype. In macrophages, BVR is regulated by its substrate BV which leads to activation of the PI3K–Akt-IL-10 axis and inhibition of TLR4 expression via direct binding of BVR to the TLR4 promoter. In this review, we will summarize recent findings on the role of BVR and the bile pigments in inflammation in context with its activity as an enzyme, receptor, and transcriptional regulator.

show abstract

Section: Bvr-identification and Characterizationmentioning

confidence: 99%

Go Green: The Anti-Inflammatory Effects of Biliverdin Reductase

Węgiel¹,

Otterbein²

2012

Front. Pharmacol.

118

View full text Add to dashboard Cite

show abstract

“…50-52°C (with decomposition). 1 H-NMR (300 MHz, l, CDCl 3 ): 10.4 (broad s, 1H, pyrrole NH), 10.0 (sharper broad s, 1H, lactam NH), 6.2 (broad s, 1H, amide NH), 6.05 (s, 1H, CH ), 3.6 (s, ca. 180H, polymeric -CH 2 -), 3.3 (s, 3H, polymeric O CH 3 ), 2.7 (t, 2H, (CH 2 CH 2 COO ), 2.5 (q, 2H, CH 2 CH 3 ), 2.3 (t+ s, 2H+ 3H, CH 2 CH 2 COO , C3% or C5% CH 3 ), 2.1 (s, 3H, C5% or C3% CH 3 ), 1.9 (s, 3H, C3 CH 3 ), 1.2 (t, 3H, CH 2 CH 3 ).…”

Section: Xanthobilirubic Acid Monomethoxy Polyethylene Glycol Amide (mentioning

confidence: 99%

“…The aqueous solubility of the verdin 2-MPEGA makes it an adequate substrate for the study of the reduction step of the biliverdin reductase system [9]. Frydman et al studied the substrate specificity and kinetics by this enzyme [10]. After examining a series of synthetic biliverdins with a varying number of propionate and acetate chains, they found that the presence of at least two propionates in the biliverdin structure was needed for substrate activity.…”

mentioning

confidence: 99%

Synthesis of water-soluble bile pigments bound to amine-ended monomethoxypolyethyleneglycol: thiol addition and attempted enzymatic reduction of a bilindione derivative

Salamí¹,

Mazo

Lightner

et al. 1997

CMLS, Cell. mol. life sci.

View full text Add to dashboard Cite

The water-soluble amide to an NH2-ended monomethoxypolyethyleneglycol (MPEG-NH2, molecular mass of about 2000) of the dipyrrinone xanthobilirubic acid (XBR, 1) and the bis-amides of mesobiliverdin-XIII alpha (MBV, 2) and mesobilirubin-XIII alpha (MBR, 3) have been prepared with high yields. Contrary to what is observed with biliverdin-IX alpha, 4, the enzymatic reduction of the mesobiliverdin derivative 2-MPEGA to the corresponding mesobilirubin 3-MPEGA by the soluble biliverdin reductase/NADPH system in pH 7.4 aqueous phosphate does not occur. In contrast, thiol addition to 2-MPEGA and to 4 under similar conditions is immediate, although this equilibrium is slightly less favourable for 2-MPEGA. These results enable us to discount the intrinsically low reactivity of 2-MPEGA towards thiols as the reason for its lack of enzymatic reduction, and suggest instead that this particular mesobiliverdin cannot fit properly into the enzyme binding site, either because of steric hindrance or the lack of the two propionic acid groups.

show abstract

“…Molecular form 3 of biliverdin reductase was obtained from CoClr treated rats and purified as described [9]. The peroxisomal NAD+dependent dehydrogenase was prepared as described elsewhere [4].…”

Section: Enume Preparationsmentioning

confidence: 99%

The in vivo and in vitro oxidation of molecular form 1 of biliverdin reductase to molecular form 3 by diamide

Tomaro

Frydman

1990

FEBS Letters

Self Cite

View full text Add to dashboard Cite

The in vivo and in vitro oxidation of molecular form 1 of biliverdin reductase to molecular form 3 by diamide Administration of phenylhydrazine to rats converted molecular form f of the liver biliverdia reductase into its disulgde bridN dimer (molecular farm 3). This oxidative dimerization was shown not to be mediated by the NAD"-dependent dehydrogenase [(1984) Rio&em. Riophys. Res. Commun. I2 1,2492541. Administration of diamide produced the same conversion, Although hepatic levels of GSH alsa decreased, no mixed disulfides of the reductase and GSH could be detected. Administration of the antioxidants allopurinol and a-tocopherol together with the diamide did not at%ct this conversion of molecular forms produced by the latter. The diamide also axidized molecular form 1 of biliverdin mductase in vitro and molecular form 3 was formed. The ohemical oxidation took place at a high rate and was partially inhibited by GSH but not by cysteine.

show abstract

Biliverdin reductase: substrate specificity and kinetics

Cited by 21 publications

References 17 publications

Go Green: The Anti-Inflammatory Effects of Biliverdin Reductase

Go Green: The Anti-Inflammatory Effects of Biliverdin Reductase

Synthesis of water-soluble bile pigments bound to amine-ended monomethoxypolyethyleneglycol: thiol addition and attempted enzymatic reduction of a bilindione derivative

The in vivo and in vitro oxidation of molecular form 1 of biliverdin reductase to molecular form 3 by diamide

Contact Info

Product

Resources

About