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Identification of a Carboxyl group at the Active Site of Barley MaIt Phosphatase

Document Type

Research

Abstract

The dependence of the maximal velocity, V_m with pH for barley malt phosphatase has been studied from pH 4.0 to 5.4. The data show that an ionizable group in the enzyme-substrate complex with a pK₂ of 4-4.6 is important for enzymic activity. These results suggest strongly the involvement of a carboxyl group of a glutamic or aspartic acid residue at the active site of this enzyme.

Publication Date

1965

Journal Title

Proceedings of the Iowa Academy of Science

Volume

Issue

First Page

113

Last Page

116

Copyright

Language

File Format

application/pdf

Recommended Citation

Aherne, F. X.; Bennett, G. A.; Berner, D. L.; Burke, M. E.; Busch, N. E.; Carrothers, W.; Chan, K-P.; Conradie, A. R.; Daniels, J. D.; Dunn, F. L.; Feider, M.; Frobish, L. T.; Ganfield, M. W.; Hallahan, M. E.; Hills, D. C.; Hodgin, L. A.; Howard, J. R.; Hume, D. J.; Huntington, J. L.; Husted, R. R.; Isenhart, J. W.; Johnson, R. J.; Kao, W-H.; Killos, P. J.; Lachica, R. D. F.; Linden, J. C.; Nelson, D. K.; Patnode, S. C.; Qureshi, M. C.; Rambo, R. S.; Richardson, L. F.; Rose, R. J.; Sair, R. A.; Scharffenberg, S.; Shonka, M. L.; Smith, R. L.; Stifel, F. B.; Treadwell, G. E. Jr.; Tsuda, Y.; Wise, J. L. Jr.; and Fisher, T. L. (1965) "Identification of a Carboxyl group at the Active Site of Barley MaIt Phosphatase," Proceedings of the Iowa Academy of Science, 72(1), 113-116.
Available at: https://scholarworks.uni.edu/pias/vol72/iss1/19

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