Hippuryl-L-phenylalanine has been used as a substrate for screening carboxypeptidase activity in Trogoderma granarium,[1]Bactrocera oleae Gmelin[2] and Apodiphus amygdali.[3]
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Hippuryl-L-phenylalanine is a substrate for carboxypeptidase A enzyme.[4]
We have investigated the function of Tyr248 using bovine wild-type CPA and its Y248F and Y248A mutants to find that the K(M) values were increased by 4.5-11-fold and the k(cat) values were reduced by 4.5-10.7-fold by the replacement of Tyr248
This paper presents stable carboxypeptidase A (CPA)-glyoxyl derivatives, to be used in the controlled hydrolysis of proteins. They were produced after immobilizing-stabilizing CPA on cross-linked 6% agarose beads, activated with low and high concentrations of aldehyde groups, and different immobilization
Biochemical and biophysical research communications, 132(2), 681-687 (1985-10-30)
Carboxypeptidase A was incubated at -60 degrees C with an excess of O-(trans-p-chlorocinnamoyl)-L-phenyllactate, O-(hippuryl)-glycolate or N-(hippuryl)-L-phenylalanine. After rapid denaturation with trichloracetic acid the precipitated protein was reduced with [3H]NaCNBH3. 3H Labeled enzyme was isolated by gel chromatography on Sephadex G-25.
Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.
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