Discovery and development of direct thrombin inhibitors the binding site for the globular amino-terminal domain and exosite 1 is the binding site for the acidic carboxy-terminal domain of hirudin. Native hirudin, a 65-amino-acid polypeptide, is produced in the parapharyngeal glands of medicinal leeches. Hirudins today are produced by recombinant biotechnology using yeast. These recombinant hirudins lack a sulfate group at Tyr-63 and are therefore called desulfatohirudins. They have a 10-fold lower binding affinity to thrombin compared to native hirudin, but remain a highly specific inhibitor of thrombin and have an inhibition constant for thrombin in the picomolar range. Renal clearance and degradation account for the most part
Naturally occurring phenols human gene encoding a phenol UDP glucuronosyltransferase active on simple phenols. The enzyme encoded by the gene UGT1A8 has glucuronidase activity with many substrates including coumarins, anthraquinones and flavones. Naturally occurring phenols In biochemistry, naturally occurring phenols refers to phenol functional group that is found in natural products. Phenolic compounds are are produced by plants and microorganisms. Organisms sometimes synthesize phenolic compounds in response to ecological pressures such as pathogen and insect attack, UV radiation and wounding. As they are present in food consumed in human diets and in plants used in traditional medicine of several cultures, their role in