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L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-alanyl-L-phenylalanyl- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

65356-79-8

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65356-79-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 65356-79-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,5,3,5 and 6 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 65356-79:
(7*6)+(6*5)+(5*3)+(4*5)+(3*6)+(2*7)+(1*9)=148
148 % 10 = 8
So 65356-79-8 is a valid CAS Registry Number.

65356-79-8Downstream Products

65356-79-8Relevant academic research and scientific papers

Chemo-enzymatic synthesis of optically active amino acids and peptides

Chen, Shui-Tein,Wang, Kung-Tsung

, p. 301 - 311 (2007/10/03)

The industrial alkaline protease, alcalase, is stable and active in a high concentration of organic solvents and useful as a biocatalyst for (i) diastereoselective hydrolysis of peptide esters and preparation of racemization-free peptides; (ii) selective incorporation of esters of D-amino acid into peptides in t-butanol via a selective hydrolysis of esters of D,L-amino acid, followed by using the unhydrolyzed D-esters as a nucleophile in a kinetically controlled peptide bond formation; (iii) resolution of esters of amino acid in 95% t-butanol/5% water, followed by saponification of the unreacted esters to offer both enantiomers with high yield and optical purity; (iv) completely resolve amino-acid esters with high yield and optical purity via in situ racemization of the unreacted antipode catalyzed by pyridoxal 5-phosphate; (v) cryobioorganic synthesis of peptides with increased yields 15%-40% of peptide bond formation by reaction at 5 °C instead of 25-30 °C of a kinetically controlled enzymatic reaction in alcohols.

Kinetically Controlled Peptide Bond Formation in Anhydrous Alcohol Catalyzed by the Industrial Protease Alcalase

Chen, Shui-Tein,Chen, Shiah-Yun,Wang, Kung-Tsung

, p. 6960 - 6965 (2007/10/02)

The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol).Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol (ethanol, 2-methyl-2-propanol).Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates.Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles.Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95percent yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48percent in 2-methyl-2-propanol containing 4.86percent water.

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