Document Detail

Azotobacter vinelandii citrate synthase.
MedLine Citation:
PMID:  7819205     Owner:  NLM     Status:  MEDLINE    
We have purified the citrate synthase from Azotobacter vinelandii and have determined that the size of the subunit is 48,000 Da and the structure of the holoenzyme is a hexamer. This contrasts with earlier estimates that indicate a 58,000 Da subunit and a tetrameric structure. In addition, the enzyme is allosteric with a Hill coefficient of 1.5 and is inhibited by NADH. The Hill coefficient is changed to about 1 by high ionic strength and AMP. The enzyme is thus similar to the citrate synthases of many other Gram-negative, facultative, anaerobic organisms. In addition, the amino acid sequence of about 100 residues has been determined and found to be highly similar to the sequence of Pseudomonas aeruginosa citrate synthase.
M Rault-Leonardon; M A Atkinson; C A Slaughter; C R Moomaw; P A Srere
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  34     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1995 Jan 
Date Detail:
Created Date:  1995-02-16     Completed Date:  1995-02-16     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  257-63     Citation Subset:  IM    
Pre-Clinical Science Unit, Department of Veterans Affairs Medical Center, Dallas, Texas 75216.
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MeSH Terms
Amino Acid Sequence
Azotobacter vinelandii / enzymology*
Citrate (si)-Synthase / antagonists & inhibitors,  chemistry,  isolation & purification,  metabolism*
Electrophoresis, Polyacrylamide Gel
Molecular Sequence Data
Molecular Weight
NAD / pharmacology
Sequence Homology, Amino Acid
Grant Support
Reg. No./Substance:
53-84-9/NAD; EC (si)-Synthase

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