phosphomonoesterase

• phosphormonoesterase

phospho- +‎ monoester +‎ -ase

• (General American) IPA^(key): /ˌfɑsfoʊˌmɑnoʊˈɛstəˌɹeɪs/

phosphomonoesterase (countable and uncountable, plural phosphomonoesterases)

1. (biochemistry) A phosphoric monoester hydrolase; an enzyme that catalyzes the hydrolysis of O-P bonds by nucleophilic attack of phosphorus by cysteine residues or coordinated metal ions.
   • 1955, John B. Wolff and Nathan O. Kaplan, “d-Mannitol 1-Phosphate Dehydrogenase from Escherichia Coli”, in The Journal of General Physiology, page 850:

     Dr. L. Shuster kindly furnished samples of prostatic acid phosphomonoesterase prepared according to the procedure of Markham and Smith.

   • 1965, Findlay E. Russell, “Venomous Animals and Their Toxins”, in Annual Report of the Board of Regents of the Smithsonian Institution: Showing the Operations, Expenditures, and Condition of the Institution for the Year Ended June 30 1964, pages 479–80:

     The venoms of snakes […] contain many enzymes, some of which, such as the proteases, phosphomonoesterase, phosphodiesterase, L–amino acid oxidase, 5-nucleotidase, cholinesterase, ribonuclease, desoxyribonuclease, ATPase, DNPase, and hyaluronidase are being used by the biochemist, pharmacologist, and physician.

   • 1976, D. B. Gelman, D. K. Hayes, and M. S. Schechter, “Ammonium Sulfate Activation of Phosphodiesterase in Homogenates of Larvae of the European Corn Borer”, in Proceedings of the Society for Experimental Biology and Medicine, volume 152, page 170:

     We first noted activation by high concentrations of ammonium sulfate […] when we attempted to purify cyclic adenosine monophosphatase (c-AMP-ase), phosphomonoesterase, and phosphodiesterase by the method of Robison.