Azotobacter vinelandii citrate synthase.
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.
Rault-Leonardon
M
M
Pre-Clinical Science Unit, Department of Veterans Affairs Medical Center, Dallas, Texas 75216.
Atkinson
M A
MA
Slaughter
C A
CA
Moomaw
C R
CR
Srere
P A
PA
D000595:Amino Acid Sequence; D016948:Azotobacter vinelandii / Q000201:enzymology*; D002950:Citrate (si)-Synthase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D014461:Ultracentrifugation
D009243:NAD; D002950:Citrate (si)-Synthase