Genetic and biochemical investigations on bacterial catabolic pathways for lignin-derived aromatic compounds

被引:384
作者
Masai, Eiji [1 ]
Katayama, Yoshihiro
Fukuda, Masao
机构
[1] Nagaoka Univ Technol, Dept Bioengn, Niigata 9402188, Japan
[2] Tokyo Univ Agr & Technol, Grad Sch Bioapplicat & Syst Engn, Koganei, Tokyo 1848588, Japan
关键词
lignin biodegradation; Sphingomonas; glutathione S-transferases; extradiol dioxygenases; tetrahydrofolate-dependent O-demethylases;
D O I
10.1271/bbb.60437
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
Lignins are the most abundant aromatic compounds in nature, and their decomposition is essential to the terrestrial carbon cycle. White rot fungi secreting phenol oxidases are assumed to be involved in the initial degradation of native lignin, whereas bacteria play a main role in the mineralization of lignin-derived low-molecular-weight compounds in soil. There are a number of reports on the degradation pathways for lignin-derived aromatic compounds, but their catabolism has not been enzymatically or genetically characterized. Sphingomonas paucimobilis SYK-6 is one of the best-characterized lignin-degrading bacteria. It can grow on a wide variety of lignin-related biaryls and monoaryls, including beta-aryl ether, biphenyl, diarylpropane, and phenylpropane. These compounds are degraded via the protocatechuate (PCA) 4,5-cleavage pathway or multiple 3-O-methylgallate (3MGA) catabolic pathways. In this review, the enzyme systems for beta-aryl ether and biphenyl degradation, O demethylation linked with one carbon metabolism, the PCA 4,5-cleavage pathway, and the multiple 3MGA catabolic pathways in SYK-6 are outlined.
引用
收藏
页码:1 / 15
页数:15
相关论文
共 104 条
[41]   Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1 [J].
Maruyama, K ;
Shibayama, T ;
Ichikawa, A ;
Sakou, Y ;
Yamada, S ;
Sugisaki, H .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2004, 68 (07) :1434-1441
[42]   Cloning, sequencing, and expression of the gene encoding 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae NGJ1 [J].
Maruyama, K ;
Miwa, M ;
Tsujii, N ;
Nagai, T ;
Tomita, N ;
Harada, T ;
Sobajima, H ;
Sugisaki, H .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2001, 65 (12) :2701-2709
[44]   PURIFICATION AND PROPERTIES OF 4-HYDROXY-4-METHYL-2-OXOGLUTARATE ALDOLASE FROM PSEUDOMONAS-OCHRACEAE GROWN ON PHTHALATE [J].
MARUYAMA, K .
JOURNAL OF BIOCHEMISTRY, 1990, 108 (02) :327-333
[45]   PURIFICATION AND PROPERTIES OF 2-PYRONE-4,6-DICARBOXYLATE HYDROLASE [J].
MARUYAMA, K .
JOURNAL OF BIOCHEMISTRY, 1983, 93 (02) :557-565
[46]   ISOLATION AND IDENTIFICATION OF THE REACTION-PRODUCT OF ALPHA-HYDROXY-GAMMA-CARBOXYMUCONIC EPSILON-SEMIALDEHYDE DEHYDROGENASE [J].
MARUYAMA, K .
JOURNAL OF BIOCHEMISTRY, 1979, 86 (06) :1671-1677
[47]   PURIFICATION AND PROPERTIES OF ALPHA-HYDROXY-GAMMA-CARBOXYMUCONIC EPSILON-SEMIALDEHYDE DEHYDROGENASE [J].
MARUYAMA, K ;
ARIGA, N ;
TSUDA, M ;
DEGUCHI, K .
JOURNAL OF BIOCHEMISTRY, 1978, 83 (04) :1125-1134
[48]   Roles of the enantioselective glutathione S-transferases in cleavage of β-aryl ether [J].
Masai, E ;
Ichimura, A ;
Sato, Y ;
Miyauchi, K ;
Katayama, Y ;
Fukuda, M .
JOURNAL OF BACTERIOLOGY, 2003, 185 (06) :1768-1775
[49]   A BACTERIAL ENZYME DEGRADING THE MODEL LIGNIN COMPOUND BETA-ETHERASE IS A MEMBER OF THE GLUTATHIONE-S-TRANSFERASE SUPERFAMILY [J].
MASAI, E ;
KATAYAMA, Y ;
KUBOTA, S ;
KAWAI, S ;
YAMASAKI, M ;
MOROHOSHI, N .
FEBS LETTERS, 1993, 323 (1-2) :135-140
[50]   A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate [J].
Masai, E ;
Sasaki, M ;
Minakawa, Y ;
Abe, T ;
Sonoki, T ;
Miyauchi, K ;
Katayama, Y ;
Fukuda, M .
JOURNAL OF BACTERIOLOGY, 2004, 186 (09) :2757-2765