Z-Phe-Leu
Z-Phe-Leu structure
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Common Name | Z-Phe-Leu | ||
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| CAS Number | 4313-73-9 | Molecular Weight | 412.47900 | |
| Density | 1.193g/cm3 | Boiling Point | 674.4ºC at 760mmHg | |
| Molecular Formula | C23H28N2O5 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 361.7ºC | |
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Amphipathic property of free thiol group contributes to an increase in the catalytic efficiency of carboxypeptidase Y.
Eur. J. Biochem. 269 , 3220-3225, (2002) Cys341 of carboxypeptidase Y, which constitutes one side of the solvent-accessible surface of the S1 binding pocket, was replaced with Gly, Ser, Asp, Val, Phe or His by site-directed mutagenesis. Kinetic analysis, using Cbz-dipeptide substrates, revealed that... |
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Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates.
J. Ind. Microbiol. Biotechnol. 35 , 41-47, (2008) Effects of the enzymes in Actinomucor elegans extract and the enzyme Alcalase 2.4L on debittering the soybean protein hydrolysates were investigated. When the protein was treated only with the latter, a strong bitterness formed; but it decreased if the protei... |
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Characterization of a bifunctional aminoacylase/carboxypeptidase from radioresistant bacterium Deinococcus radiodurans R1.
J. Biotechnol. 128 , 322-334, (2007) The gene encoding a Deinococcus radiodurans R1 bifunctional aminoacylase/carboxypeptidase (DR_ACY/CP) was amplified by polymerase chain reaction and cloned into pQE-30 to generate pQE-DRAC. The cloned gene consists of an open reading frame of 1197 bp encoding... |
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Cathepsin A-like activity is possibly the main acidic carboxypeptidase in human platelets.
Platelets 8 , 355-360, (1997) Human platelets were investigated for activity of the acidic carboxypeptidases: cathepsin A, lysosomal carboxypeptidase B and prolyl-carboxypeptidase. It was found that the main acidic carboxypeptidase in human platelets had cathepsin A activity. No activity ... |
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Purification and characterization of a carboxypeptidase from squid hepatopancreas (Illex illecebrosus).
J. Agric. Food Chem. 49 , 5019-5030, (2001) The hepatopancreas of squid (Illex illecebrosus) extract contains a wide range of carboxypeptidase (CP) activities based on hydrolysis of N-CBZ-dipeptide substrates. SDS-PAGE zymograms with N-CBZ-Phe-Leu substrate revealed three activity zones (CP-I, 23 kDa; ... |