Bicarbonate is a recycling substrate for cyanase
Cyanase catalyzes HCO/sub 3//sup -/-dependent decomposition of cyanate to NH/sub 4//sup +/ and HCO/sub 3//sup -/. Previous studies provided evidence that carbamate is an initial product and that the kinetic mechanism is rapid equilibrium random (HCO/sub 3//sup -/ serving as substrate as opposed to activator). Direct evidence for this mechanism was obtained in this study by (1) identifying the products formed from (/sup 14/C)HCO/sub 3//sup -/ or (/sup 14/C)OCN/sup -/, (2) identifying the products formed from (/sup 13/C)HCO/sub 3//sup -/ in the presence of (/sup 18/O)H/sub 2/O, and (3) determining whether CO/sub 2/ or HCO/sub 3//sup -/ serve as substrate and are formed as product. Carbon dioxide (not HCO/sub 3//sup -/) is produced in stoichiometric amounts from both HCO/sub 3//sup -/ and OCN/sup -/. Bicarbonate (not CO/sub 2/) is the substrate. Oxygen-18 from (/sup 18/O)H/sub 2/O is not incorporated into CO/sub 2/ formed from either HCO/sub 3//sup -/ or OCN/sup -/. These results indicate that decomposition of cyanate is not a hydrolysis reaction and that HCO/sub 3//sup -/ functions as a substrate.
- Research Organization:
- Univ. of Minnesota, Duluth
- OSTI ID:
- 6074987
- Report Number(s):
- CONF-870644-; TRN: 87-037117
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ACID CARBONATES
BIOLOGICAL FUNCTIONS
LYASES
SUBSTRATES
CARBON 13
CARBON 14 COMPOUNDS
CARBON DIOXIDE
OXYGEN 18
STOICHIOMETRY
TRACER TECHNIQUES
WATER
CARBON COMPOUNDS
CARBON ISOTOPES
CARBON OXIDES
CHALCOGENIDES
ENZYMES
EVEN-EVEN NUCLEI
EVEN-ODD NUCLEI
FUNCTIONS
HYDROGEN COMPOUNDS
ISOTOPE APPLICATIONS
ISOTOPES
LABELLED COMPOUNDS
LIGHT NUCLEI
NUCLEI
OXIDES
OXYGEN COMPOUNDS
OXYGEN ISOTOPES
STABLE ISOTOPES
550201* - Biochemistry- Tracer Techniques