Abstract:
:The fructose-1,6-bisphosphate aldolase gene from the thermophilic bacterium, Anoxybacillus gonensis G2, was cloned and sequenced. Nucleotide sequence analysis revealed an open reading frame coding for a 30.9 kDa protein of 286 amino acids. The amino acid sequence shared approximately 80-90% similarity to the Bacillus sp. class II aldolases. The motifs that are responsible for the binding of a divalent metal ion and catalytic activity completely conserved. The gene encoding aldolase was overexpressed under T7 promoter control in Escherichia coli and the recombinant protein purified by nickel affinity chromatography. Kinetic characterization of the enzyme was performed at 60 degrees C, and K(m) and V(max) were found to be 576 microM and 2.4 microM min(-1) mg protein(-1), respectively. Enzyme exhibits maximal activity at pH 8.5. The activity of enzyme was completely inhibited by EDTA.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Ertunga NS,Colak A,Belduz AO,Canakci S,Karaoglu H,Sandalli Cdoi
10.1093/jb/mvm085subject
Has Abstractpub_date
2007-06-01 00:00:00pages
817-25issue
6eissn
0021-924Xissn
1756-2651pii
mvm085journal_volume
141pub_type
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