Adenylyl cyclase activity of Cya1 from the cyanobacterium Synechocystis sp. strain PCC 6803 is inhibited by bicarbonate.
Bicarbonate stimulates the activities of several class III adenylyl cyclases studied to date. However, we show here that bicarbonate decreased V(max) and substrate affinity in Cya1, a major adenylyl cyclase in the cyanobacterium Synechocystis sp. strain PCC 6803. This indicates that manifestation of the bicarbonate responsiveness is specifically modulated in Cya1.
Laboratory for Photo-Biology, RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, Aramaki, Aoba, Sendai, Japan. shmasuda@bio.titech.ac.jp
Shinji
S
Masuda
Taka-aki
TA
Ono
D000255:Adenosine Triphosphate / Q000378:metabolism; D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D001639:Bicarbonates / Q000494:pharmacology*; D020134:Catalytic Domain; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D051381:Rats; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D046939:Synechocystis / Q000201:enzymology*
D000067956:Adenylyl Cyclase Inhibitors; D001426:Bacterial Proteins; D001639:Bicarbonates; D000255:Adenosine Triphosphate; D000262:Adenylyl Cyclases