Document Detail


Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities.
MedLine Citation:
PMID:  9882445     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The deduced primary sequence (cbbL and cbbS) of form I ribulose 1, 5-bisphosphate carboxylase/oxygenase (rubisco) from Bradyrhizobium japonicum places this enzyme within the Type IC subgroup of red-like rubisco enzymes. In addition, B. japonicum appears to organize most of the structural genes of the Calvin-Benson-Bassham (CBB) pathway in at least one major operon. Functional expression and characterization of the B. japonicum and Xanthobacter flavus enzymes from this group revealed that these molecules exhibit diverse kinetic properties despite their relatively high degree of sequence relatedness. Of prime importance was the fact that these closely related enzymes exhibited CO2 and O2 substrate specificities that varied from relatively low values [tau = (VcKo)/(VoKc) = 45] to values that approximated those obtained for higher plants (tau = 75). These results, combined with the metabolic and genetic versatility of the organisms from which these enzymes were derived, suggest a potential rich resource for future biological selection and structure-function studies aimed at elucidating structural features that govern key enzymological properties of rubisco.
Authors:
K M Horken; F R Tabita
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  361     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1999 Jan 
Date Detail:
Created Date:  1999-02-11     Completed Date:  1999-02-11     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  183-94     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Affiliation:
Department of Microbiology, Ohio State University, 484 West 12th Avenue, Columbus, Ohio, 43210-1292, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AF041820
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  isolation & purification
Bradyrhizobium / enzymology,  genetics
Carbon Dioxide / metabolism*
Enzyme Activation / genetics
Genes, Bacterial
Gram-Negative Aerobic Bacteria / enzymology
Isoenzymes / chemistry,  metabolism
Models, Molecular
Molecular Sequence Data
Oxygen / metabolism*
Recombinant Proteins / biosynthesis,  isolation & purification
Ribulose-Bisphosphate Carboxylase / chemistry*,  genetics,  metabolism*
Sequence Deletion
Substrate Specificity
Grant Support
ID/Acronym/Agency:
GM-24497/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Isoenzymes; 0/Recombinant Proteins; 124-38-9/Carbon Dioxide; 7782-44-7/Oxygen; EC 4.1.1.39/Ribulose-Bisphosphate Carboxylase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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