Hippuryl-Phe-OH

Hippuryl-Phe-OH Structure
Hippuryl-Phe-OH structure
Common Name Hippuryl-Phe-OH
CAS Number 744-59-2 Molecular Weight 326.346
Density 1.3±0.1 g/cm3 Boiling Point 673.3±55.0 °C at 760 mmHg
Molecular Formula C18H18N2O4 Melting Point 140-144ºC
MSDS Chinese USA Flash Point 361.0±31.5 °C

Structural and functional characterization of ochratoxinase, a novel mycotoxin-degrading enzyme.

Biochem. J. 462(3) , 441-52, (2014)

Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminat...

Mast cell proteases.

Meth. Enzymol. 80 , 588, (1981)

Mechanisms for activation and inhibition of carboxypeptidase A catalyzed hydrolyses of peptides and esters.

Can. J. Biochem. 56 , 329, (1978)

3,3-Diphenylpropanoate (DPP) activates the carboxypeptidase A catalyzed hydrolysis of benzoylglycyl-L-phenylalanine (BzGly-L-Phe) (Ka = 2.1 x 10 (-3) M) and inhibits ester hydrolysis uncompetitively (K1 =2.1 X 10 (-3) M). A common modifier binding site locate...

Design of new immobilized-stabilized carboxypeptidase a derivative for production of aromatic free hydrolysates of proteins.

Biotechnol. Prog. 19(2) , 565-74, (2003)

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...

Determination of kininase I and kininase II activities in human urine by high-performance liquid chromatography.

J. Chromatogr. A. 414(2) , 423-8, (1987)

Direct chemical evidence for the mixed anhydride intermediate of carboxypeptidase A in ester and peptide hydrolysis.

Biochem. Biophys. Res. Commun. 132(2) , 681-7, (1985)

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 wit...

The role of Tyr248 probed by mutant bovine carboxypeptidase A: insight into the catalytic mechanism of carboxypeptidase A.

Biochemistry 40(34) , 10197-203, (2001)

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 with Phe for the...

Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2.

Arch. Biochem. Biophys. 332(1) , 8-18, (1996)

We are investigating the potential utility of human carboxypeptidases A in antibody-directed enzyme prodrug therapy (ADEPT). Hybridization screening of a human pancreatic cDNA library with cDNA probes that encoded either rat carboxypeptidase A1 (rCPA1) or car...

A novel [125I]iodinated carboxypeptidase A substrate detects a metallopeptidase activity distinct from carboxypeptidase A in brain.

Neuropeptides 30(1) , 13-7, (1996)

We have designed two radioactive substrates, hippuryl-L-[3H]phenylalanine and 3-(p-hydroxy, m-[125I]phenyl)propionic acid ([125I]Bolton reagent) derivative of L-arginyl-L-phenylalanine, i.e. [125I]BRF, for a highly sensitive assay of carboxypeptidase A (CPA) ...