Modification of amino acid residues in the S 1 ′ binding site of carboxypeptidase Y-Reference-Cited by-同舟云学术

Modification of amino acid residues in the S 1 ′ binding site of carboxypeptidase Y

Published:1984-01 Issue:7 Volume:49 Page:627-638
ISSN:0105-1938
Container-title:Carlsberg Research Communications
language:en
Short-container-title:Carlsberg Res. Commun.

Author:

Breddam Klaus

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/BF02907495.pdf

Reference20 articles.

1. Bai, Y., R. Hayashi &T. Hata: Kinetic studies of carboxypeptidase Y. II. Effects of substrate and products analogs on peptidase and esterase activities. J. Biochem. 77, 81–88 (1975)

2. Bai, Y. &R. Hayashi: Properties of the single sulfhydryl group of carboxypeptidase Y. Effects of alkyl and aromatic mercurials on activities towards various synthetic substrates. J. Biol. Chem. 254, 8473–8479 (1979)

3. Breddam, K.: Modification of the single sulfhydryl group of carboxypeptidase Y with mercurials. Influence on enzyme specificity. Carlsberg Res. Commun. 48, 9–19 (1983)

4. Breddam, K., S. Sørensen &M. Ottesen: Isolation of a carboxypeptidase from malted barley by affinity chromatography. Carlsberg Res. Commun. 48, 217–230 (1983)

5. Breddam, K., F. Widmer &J.T. Johansen: Amino acid methyl esters as amine components in CPD-Y catalyzed peptide synthesis. Control of side-reactions. Carlsberg Res. Commun. 48, 231–237 (1983)

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Active-site residues of procarboxypeptidase Y are accessible to chemical modification;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1994-04

2. Application of Quantitative Structure-Activity Relationship Modeling to the Evaluation of the Changes in Enzymatic Activity of Carboxypeptidase Y upon Chemical Modifications;Archives of Biochemistry and Biophysics;1993-08

3. Altering substrate preference of carboxypeptidase Y by a novel strategy of mutagenesis eliminating wild type background;"Protein Engineering, Design and Selection";1993

4. Peptide enzymatic microsynthesis, using carboxypeptidase Y as the catalyst: application to stepwise synthesis of Leu-enkephalin;Biochimie;1988-06

5. Chemical modifications of a cysteinyl residue introduced in the binding site of carboxypeptidase Y by site-directed mutagenesis;Carlsberg Research Communications;1988-01