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[Carbamoyl phosphate biosynthesis in Streptococci]
Zhurnal Mikrobiologii, Epidemiologii I Immunobiologii
|July 1, 1982
Summary
Nine streptococcal strains synthesize carbamoyl phosphate using carbamate kinase. Activity varied by serological group, with Group A showing the highest and Group D the lowest enzyme activity.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Streptococci are common bacteria with diverse serological groups.
- Carbamoyl phosphate is a key intermediate in amino acid and nucleotide biosynthesis.
- Carbamate kinase (EC 2.7.2.2) catalyzes carbamoyl phosphate synthesis.
Purpose of the Study:
- To investigate carbamate kinase activity in different streptococcal serological groups.
- To quantify the synthesis of carbamoyl phosphate by selected streptococcal strains.
Main Methods:
- Nine streptococcal strains from serological groups A, B, C, and D were cultured.
- Carbamoyl phosphate synthesis was measured by the production of citrulline.
- Enzyme activity was determined using ammonium hydrocarbonate, ATP, and ornithine transcarbamoylase.
Main Results:
- All nine streptococcal strains synthesized carbamoyl phosphate.
- Carbamate kinase activity varied significantly across serological groups.
- Group A streptococci exhibited the highest specific activity (13 nmol/min/mg biomass), while Group D showed the lowest (0.5 nmol/min/mg biomass).
Conclusions:
- Streptococcal carbamate kinase activity is quantitatively different among serological groups.
- Group A streptococci possess higher carbamate kinase activity compared to other groups studied.
- These findings highlight metabolic diversity within streptococcal species relevant to carbamoyl phosphate synthesis.