Document Detail


Biliverdin reductase: substrate specificity and kinetics.
MedLine Citation:
PMID:  3689807     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 by the enzyme either. The presence of two propionates in the biliverdin structure gave a biliverdin with substrate activity. Increasing the number of propionates to four, as in coprobiliverdins, did not affect substrate activity, while the octaacid urobiliverdins were also good substrates of the enzymes. The beta isomer of urobiliverdin III and coprobiliverdin III were reduced at much higher rates by molecular form 3 of the enzyme as compared to molecular form 1, a fact which had already been observed with the beta isomer of biliverdins IX, XIII and hematobiliverdin. All the biliverdins mentioned above were readily reduced to bilirubins by sodium borohydride. The purified molecular forms 1 and 3 displayed sigmoidal kinetics with most of the biliverdins tested. The data were analyzed by nonlinear regression in a microcomputer and it was found that they fitted a model of a moderate cooperative dimer where both ES and ES2 are catalytically active. The Vm, Ks and the Hill numbers, nH, for biliverdin IX alpha and beta, hematobiliverdin IX alpha and beta, and several synthetic biliverdin isomers are given. Molecular form 2 showed classical Michaelian kinetics.
Authors:
R B Frydman; M L Tomaro; J Rosenfeld; J Awruch; L Sambrotta; A Valasinas; B Frydman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  916     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1987 Dec 
Date Detail:
Created Date:  1988-02-08     Completed Date:  1988-02-08     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  500-11     Citation Subset:  IM    
Affiliation:
Facultad de Farmacia y Bioquimica, Universidad de Buenos Aires, Argentina.
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MeSH Terms
Descriptor/Qualifier:
Algorithms
Animals
Biliverdine / analogs & derivatives,  metabolism
Isoenzymes / metabolism
Kinetics
Oxidoreductases / metabolism*
Oxidoreductases Acting on CH-CH Group Donors*
Rats
Substrate Specificity
Grant Support
ID/Acronym/Agency:
GM-11973/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Isoenzymes; 114-25-0/Biliverdine; EC 1.-/Oxidoreductases; EC 1.3.-/Oxidoreductases Acting on CH-CH Group Donors; EC 1.3.1.24/biliverdin reductase

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