MOLECULAR AND ENZYMATIC-PROPERTIES OF AN ASPARTIC PROTEINASE FROM RHIZOPUS HANGCHOW

被引：15

作者：

ICHISHIMA, E

OJIMA, M

YAMAGATA, Y

HANZAWA, S

NAKAMURA, T

机构：

[1] TOHOKU UNIV,FAC AGR,DEPT APPL BIOL CHEM,MOLEC ENZYMOL LAB,AOBA KU,SENDAI,MIYAGI 191,JAPAN

[2] TOSOH CO LTD,BIOTECHNOL RES LABS,AYASE,KANAGAWA 252,JAPAN

[3] SNOW BRAND MILK PROD CO LTD,TECH RES LABS,KAWAGOE,SAITAMA 350,JAPAN

来源：

PHYTOCHEMISTRY | 1995年 / 38卷 / 01期

关键词：

RHIZOPUS; FUNGUS; PROTEASE; ASPARTIC PROTEINASE; RHIZOPUSPEPSIN; SPECIFICITY;

D O I：

10.1016/0031-9422(94)00552-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An aspartic proteinase, rhizopuspepsin (EC 3.4.23.21), from Rhizopus hangchow was purified. The M(r) and isoelectric point were determined as ca 37000 and 4.5, respectively. The first 19 amino acids in the N-terminal region were SGSGVVPMTDYEYDIEYYG. The contents of the alpha-helix, beta-structure and random coil were calculated to be ca 7.5, 88.9 and 2.7%, respectively. The enzyme can activate trypsinogen at pH 3.0. The activity was completely inactivated by pepstatin A. The specificity and mode of action of the enzyme were investigated with oxidized insulin B-chain at pH 3. The enzyme hydrolysed primarily two peptide bonds, the Leu(15)-Tyr(16) bond and the Tyr(16)-Leu(17) bond, while additional cleavage of the bonds, Ala(14)-Leu(15) and Phe(24)-Phe(25) was also noted.

引用

页码：27 / 30

页数：4

共 45 条

[1] MECHANISM OF ACTIVATION OF TRYPSINOGEN - ROLE OF 4 N-TERMINAL ASPARTYL RESIDUES [J].