![]() Hippuryl-Phe-OH structure
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Common Name | Hippuryl-Phe-OH | ||
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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... |
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Mast cell proteases.
Meth. Enzymol. 80 , 588, (1981)
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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... |
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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... |
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Determination of kininase I and kininase II activities in human urine by high-performance liquid chromatography.
J. Chromatogr. A. 414(2) , 423-8, (1987)
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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... |
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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... |
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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... |
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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) ... |