Ketohexokinase (ATP:D-fructose 1-phosphotransferase) from a halophilic archaebacterium, Haloarcula vallismortis: purification and properties

Author:

Rangaswamy V1,Altekar W1

Affiliation:

1. Radiation Biology and Biochemistry Division, Bhabha Atomic Research Centre, Bombay, India.

Abstract

Ketohexokinase (ATP:D-fructose 1-phosphotransferase [EC 2.7.1.3]), detected for the first time in a prokaryote, i.e., the extreme halophile Haloarcula vallismortis, was isolated and characterized from the same archaebacterium. This enzyme was characterized with respect to its molecular mass, amino acid composition, salt dependency, immunological cross-reactivity, and kinetic properties. Gel filtration and sucrose density gradient centrifugation revealed a native molecular mass of 100 kDa for halobacterial ketohexokinase, which is larger than its mammalian counterpart. The enzyme could be labeled by UV irradiation in the presence of [ gamma-32P]ATP, suggesting the involvement of a phosphoenzyme intermediate. Other catalytic features of the enzyme were similar to those of its mammalian counterparts. No antigenic cross-reactivity could be detected between the H. vallismortis ketohexokinase and the ketohexokinases from different rat tissues.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference35 articles.

1. Altekar W. Personal communication.

2. Indication of a modified EMP pathway for fructose breakdown in a halophilic archaebacterium;Altekar W.;FEMS Microbiol. Lett.,1990

3. Ketohexokinase (ATP: Dfructose 1-phosphotransferase) initiates fructose breakdown via the modified EMP pathway in a halophilic archaebacterium;Altekar W.;FEMS Microbiol. Lett.,1991

4. Degradation of endogenous fructose during catabolism of sucrose and mannitol in halophilic archaebacteria;Altekar W.;Arch. Microbiol.,1992

5. The purification and properties of human liver ketohexokinase;Bais R.;Biochem. J.,1985

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