D-Tyrosine

Journal of Bacteriology, 1969, 98(1):205-214.

D-Tyrosine as a metabolic inhibitor of Bacillus subtilis.[Reference: WebLink]

The d-isomer of tyrosine(D-Tyrosine) is a potent inhibitor of growth in transformable strain 168 of Bacillus subtilis.
METHODS AND RESULTS:
A D-Tyrosine-resistant mutant of the inhibited strain was isolated which excreted l-tyrosine, had a diminished growth rate, and required l-phenylalanine to attain the growth rate of the wild-type parent. Mapping by deoxyribonucleate transformation located this resistance in the gene coding for prephenate dehydrogenase. This enzyme in the D-Tyrosine-resistant mutant was insensitive to the usual feedback inhibition exerted by l-tyrosine in extracts of strain 168. In contrast, the growth of poorly transformable strain 23 of B. subtilis, as well as that of several other Bacillus species, was not affected by the analogue.
CONCLUSIONS:
Transformation mapping demonstrated no linkage of this latter "natural resistance" to several different aromatic markers. Prephenate dehydrogenase in extracts from strain 23 was as sensitive as that from strain 168 to feedback inhibition by l-tyrosine in vitro. The relationships of the latter results to the regulation of tyrosine biosynthesis and the possible nature of strain differences in D-Tyrosine sensitivity are discussed.

Pflügers Archiv European Journal of Physiology, 1979, 379(3):245.

d-Tyrosine prevents hypertension in DOCA-saline treated uninephrectomised rats.[Reference: WebLink]

METHODS AND RESULTS:
High blood pressure in DOCA-saline treated uninephrectomised rats is prevented or even reversed by tyrosine(D-Tyrosine), tyramine or by treatments which - based on circumstantial evidence - might increase local brain tyramine concentration.

Chembiochem, 2010, 4(2-3):181-185.

D-Tyrosine as a Chiral Precusor to Potent Inhibitors of Human Nonpancreatic Secretory Phospholipase A2 (IIa) With Antiinflammatory Activity[Reference: WebLink]

Few reported inhibitors of secretory phospholipase A(2) enzymes truly inhibit the IIa human isoform (hnpsPLA(2)-IIa) noncovalently at submicromolar concentrations.
CONCLUSIONS:
Herein, the simple chiral precursor D-Tyrosine was derivatised to give a series of potent new inhibitors of hnpsPLA(2)-IIa.
CONCLUSIONS:
A 2.2-A crystal structure shows an inhibitor bound in the active site of the enzyme, chelated to a Ca(2+) ion through carboxylate and amide oxygen atoms, H-bonded through an amide NH group to His48, with multiple hydrophobic contacts and a T-shaped aromatic-group-His6 interaction. Antiinflammatory activity is also demonstrated for two compounds administered orally to rats.