A Class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei

Sandra E. D'Souza; Wijaya Altekar

doi:10.2323/jgam.44.235

The Journal of General and Applied Microbiology

Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260

A Class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei

Sandra E. D'Souza, Wijaya Altekar

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Keywords: Class II aldolase, divalent metal, EDTA, enzyme purification, fructose-1,6-bisphosphate, Haloferax mediterranei, halophilic, metal chelator

JOURNAL FREE ACCESS

1998 Volume 44 Issue 4 Pages 235-241

DOI https://doi.org/10.2323/jgam.44.235

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Abstract

Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) was purified 97-fold from a halophilic archaebacterium Haloferax mediterranei, with a specific activity of 2.8. The enzyme was characterized as a Class II aldolase on the basis of its inhibition by EDTA and other metal chelators. The enzyme had a specific requirement for divalent metal Fe²⁺ for activity. Sulfhydryl compounds enhanced aldolase activity.

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