Hydrolysis of s-2-aminoethylcysteinyl peptide bond by achromobacter protease i

Takeharu Masaki; Toshiyuki Takiya; Susumu Tsunasawa; Shigefumi Kuwahara; Fumio Sakiyama; Masami Soejima

doi:10.1080/bbb.58.215

Hydrolysis of s-2-aminoethylcysteinyl peptide bond by achromobacter protease i

Takeharu Masaki, Toshiyuki Takiya, Susumu Tsunasawa, Shigefumi Kuwahara, Fumio Sakiyama, Masami Soejima

Research output: Contribution to journal › Article › peer-review

Abstract

The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH₂, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.

Original language	English
Pages (from-to)	215-216
Number of pages	2
Journal	Bioscience, Biotechnology and Biochemistry
Volume	58
Issue number	1
DOIs	https://doi.org/10.1080/bbb.58.215
Publication status	Published - 1994 Jan 1
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

Access to Document

10.1080/bbb.58.215

Cite this

@article{50916530384b40e68ab4d24b19f8c99f,

title = "Hydrolysis of s-2-aminoethylcysteinyl peptide bond by achromobacter protease i",

abstract = "The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.",

author = "Takeharu Masaki and Toshiyuki Takiya and Susumu Tsunasawa and Shigefumi Kuwahara and Fumio Sakiyama and Masami Soejima",

year = "1994",

month = jan,

day = "1",

doi = "10.1080/bbb.58.215",

language = "English",

volume = "58",

pages = "215--216",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "1",

}

TY - JOUR

T1 - Hydrolysis of s-2-aminoethylcysteinyl peptide bond by achromobacter protease i

AU - Masaki, Takeharu

AU - Takiya, Toshiyuki

AU - Tsunasawa, Susumu

AU - Kuwahara, Shigefumi

AU - Sakiyama, Fumio

AU - Soejima, Masami

PY - 1994/1/1

Y1 - 1994/1/1

N2 - The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.

AB - The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.

UR - http://www.scopus.com/inward/record.url?scp=0028045918&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028045918&partnerID=8YFLogxK

U2 - 10.1080/bbb.58.215

DO - 10.1080/bbb.58.215

M3 - Article

C2 - 7764517

SN - 0916-8451

VL - 58

SP - 215

EP - 216

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 1

ER -

Hydrolysis of s-2-aminoethylcysteinyl peptide bond by achromobacter protease i

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this