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

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...

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Veröffentlicht in:	Journal of general and applied microbiology 1998, Vol.44(4), pp.235-241
Hauptverfasser:	D'Souza, Sandra E., Altekar, Wijaya
Format:	Artikel
Sprache:	eng
Schlagworte:	Archaea Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Brackish Class II aldolase divalent metal EDTA enzyme purification fructose-1,6-bisphosphate Fundamental and applied biological sciences. Psychology Haloferax mediterranei halophilic Marine metal chelator Miscellaneous Mission oriented research
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Zusammenfassung:	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.
ISSN:	0022-1260 1349-8037
DOI:	10.2323/jgam.44.235