PMID: 8968953Oct 1, 1996Paper

Quaternary structure, Mg2+ interactions, and some kinetic properties of the beta-galactosidase from Thermoanaerobacterium thermosulfurigenes EM1

Journal of Protein Chemistry
Reuben E HuberH Bahl

Abstract

The beta-galactosidase from Thermoanaerobacterium thermosulfurigenes EM1 was found to be a dimer with a monomer molecular weight of about 85,000. It lacks the alpha-peptide and an important alpha-helix that are both needed for dimer-dimer interaction and there is no homology in other important dimer-dimer interaction areas. These differences in structure probably account for the dimeric (rather than tetrameric) structure. Only 0.19 Mg2+ bound per monomer and Mg2+ had only small effects on the activity and heat stability. The absence of residues equivalent to Glu-416 and His-418 (two of the three ligands to Mg2+ in the beta-galactosidase from Escherichia coli) probably accounts for the low level of Mg2+ binding and the consequent lack of response to Mg2+. Both Na+ and K+ also had no effect on the activity. The enzyme activity with o-nitrophenyl-beta-D-galactopyanoside (ONPG) was very similar to that with p-nitrophenyl-beta-D-beta-D-galactopyranoside (PNPG) and the ONPG pH profile was very similar to the PNPG pH profile. These differences are in contrast to the E.coli beta-galactosidase, which dramatically discriminates between these two substrates. The lack of discrimination by the T. thermosulfurigenes beta-galactosidase could ...Continue Reading

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Citations

Oct 1, 2011·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·M Arivazhagan, D Anitha Rexalin
Aug 23, 2011·International Journal of Biological Macromolecules·Navneet BatraSonu Bhatia
Jul 25, 2014·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·M ElanthiraiyanM Arivazhagan
Dec 1, 2017·ACS Synthetic Biology·Ivan S GyulevGavin H Thomas

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