Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-lysine and L-ornithine

被引：32

作者：

Takatsuka, Y

Onoda, M

Sugiyama, T

Muramoto, K

Tomita, T

Kamio, Y

机构：

[1] Tohoku Univ, Appl Microbiol Lab, Aoba Ku, Sendai, Miyagi 9818555, Japan

[2] Tohoku Univ, Appl Bioorgan Chem Labs, Aoba Ku, Sendai, Miyagi 9818555, Japan

[3] Tohoku Univ, Labs Appl Phystochem, Grad Sch Agr Sci, Aoba Ku, Sendai, Miyagi 9818555, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1999年 / 63卷 / 06期

关键词：

Selenomonas ruminantium; lysine decarboxylase; ornithine decarboxylase; DL-alpha-difluoromethyllysine; DL-alpha-difluoromethylornithine;

D O I：

10.1271/bbb.63.1063

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：

Lysine decarboxylase (LDC; EC 4.1.1.18) of Selenomonas ruminantium is a constitutive enzyme and is involved in the synthesis of cadaverine, which is gn essential constituent of the peptidoglycan for normal cell growth. We purified the S. ruminantium LDC by an improved method including hydrophobic chromatography and studied the fine characteristics of the enzyme. Kinetic study of LDC showed that S. ruminanitum LDC decarboxylated both L-lysine and L-ornithine with similar K-m and the decarboxylase activities towards both substrates were competitively and irreversibly inhibited by DL-alpha-difluoromethylornithine, which is a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17), We also showed a drastic descent of LDC activity owing to the degradation of LDC at entry into the stationary phase of cell growth.

引用

页码：1063 / 1069

页数：7

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