Abstract
The subunit structure of jack bean urease has been unresolved in spite of many investigations. Thus far, the molecular weight for the native urease seem to range from 480,000 to 590,000 and the values for the monomer range from 30,000 to 97,000. The complete amino acid sequence of jack bean urease has been determined primarily by sequencing cyanogen bromide peptides, which were aligned by overlapping peptides obtained by lysylendopeptidase digestion of the protein and tryptic digestion of the citraconylated protein. The protein contains 840 amino acid residues in a single polypeptide chain and the subunit molecular weight calculated from the sequence is 90,790. The value of 544,740 for the hexamer, consistent with the value of 580,000 determined for intact urease by centrifugal analyses, indicated that urease consists of six subunits. Thirteen of 25 histidine residues in the urease subunit are crowded in the region between residues 479 and 607. Urease is a nickel metalloenzyme and the nickel has an essential role in catalysis by this enzyme. It is noteworthy that cysteine-592, which is recognized as essential for enzymatic activity and is related to the nickel ion in the active center, is located on this histidine-rich sequence.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Alagna L., Hasnain S. S., Piggott B., and Williams D. J. (1984). Biochem. J. 220, 591–595.
Andrews A. T., and Reithel F. J. (1970). Arch. Biochem. Biophys. 141, 538–546.
Bailey C. J., and Boulter D. (1969). Biochem. J. 113, 669–677.
Dixon N. E., Blakeley R. L., and Zerner B. (1980a), Can. J. Biochem. 58, 469–473.
Dixon N. E., Blakeley R. L., and Zerner B. (1980b). Can. J. Biochem. 58, 481–488.
Dixon N. E., Gazzola C., Asher C. J., Lee D. S. W., Blakeley R. L., and Zerner B. (1980c). Can. J. Biochem. 58, 474–480.
Dixon N. E., Hinds J. A., Fihelly A. K., Gazzola C., Winzor D. J., Blakeley R. L., and Zerner B. (1980d). Can. J. Biochem. 58, 1323–1334.
Dixon N. E., Riddles P. W., Gazzola C., Blakeley R. L., and Zerner B. (1980e). Can. J. Biochem. 58, 1335–1344.
Dixon N. E., Gazzola C., Blakeley R. L., and Zerner B. (1975). J. Am. Chem. Soc. 97, 4131–4133.
Fishbein W. N., Engler W. F., Griffin J. L., Scurzi W., and Bahr G. F. (1977). Eur. J. Biochem. 73, 185–190.
Gorin G., Mamiya G., and Chin C. C. (1967). Experientia 23, 443–445.
Hanabusa K. (1961). Nature 189, 551–553.
Liljas A., and Rossmann M. G. (1974). Annu. Rev. Biochem. 43, 475–507.
Mamiya G., and Gorin G. (1965). Biochim. Biophys. Acta 105, 382–385.
Reithel F. J. (1971). The Enzyme, Vol. 4 (Boyer P. D., ed.), Academic Press, New York, pp. 1–21.
Reithel F. J., and Robbins J. E. (1967). Arch. Biochem. Biophys. 120, 158–164.
Sakaguchi K., Mitsui K., and Kobashi K. (1983). J. Biochem. 93, 681–686.
Sumner J. B. (1926). J. Biol. Chem. 69, 435–441.
Sumner J. B., Gralen N., and Eriksson-Quensel I. B. (1938). J. Biol. Chem. 125, 37–44.
Takishima K., Mamiya G., and Hata M. (1983). In Frontiers in Biochemical and Biophysical Studies of Proteins and Membranes (Liu T., Sakakibara S., Schechter A. N., Yagi K., Yajima H., and Yasunobu K. T., eds.), Elsevier, New York, pp. 193–201.
Uehara K., and Kobashi K. (1959). Seikagaku 31, 715–721.
Author information
Authors and Affiliations
Additional information
This article was presented during the proceedings of the International Conference on Macromolecular Structure and Function, held at the National Defence Medical College, Tokorozawa, Japan, December 1985.
Rights and permissions
About this article
Cite this article
Mamiya, G., Takishima, K., Masakuni, M. et al. Complete amino acid sequence of jack bean urease. J Protein Chem 6, 55–59 (1987). https://doi.org/10.1007/BF00248827
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF00248827