| Title : Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441 - Arai_1999_Microbiology_145_2813 |
| Author(s) : Arai H , Yamamoto T , Ohishi T , Shimizu T , Nakata T , Kudo T |
| Ref : Microbiology , 145 ( Pt 10) :2813 , 1999 |
| Abstract : Comamonas testosteroni TA441 degrades 3-(3-hydroxyphenyl)propionate (3HPP) via the meta pathway. A gene cluster required for degradation of 3HPP was cloned from strain TA441 and sequenced. The genes encoding six catabolic enzymes, a flavin-type hydroxylase (mhpA), extradiol dioxygenase (mhpB), 2-keto-4-pentenoate hydratase (mhpD), acetaldehyde dehydrogenase (acylating) (mhpF), 4-hydroxy-2-ketovalerate aldolase (mhpE) and the meta cleavage compound hydrolase (mhpC), were found in this cluster, encoded in this order. mhpD and mhpF were separated by two genes, orf4 and orf5, which were not necessary for growth on 3HPP. The gene mhpR, encoding a putative transcriptional activator of the IcIR family, was located adjacent to mhpA in the opposite orientation. Disruption of the mhpB or mhpR genes affected growth on 3HPP or trans-3-hydroxycinnamate. The mhpB and mhpC gene products showed high specificity for 3-(2,3-dihydroxyphenyl)propionate (DHPP) and the meta cleavage compound produced from DHPP, respectively. |
| ESTHER : Arai_1999_Microbiology_145_2813 |
| PubMedSearch : Arai_1999_Microbiology_145_2813 |
| PubMedID: 10537203 |
| Gene_locus related to this paper: comte-mhpC |
| Gene_locus related to this paper: comte-mhpC |
Arai H, Yamamoto T, Ohishi T, Shimizu T, Nakata T, Kudo T (1999)
Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441
Microbiology
145 ( Pt 10) :2813
Arai H, Yamamoto T, Ohishi T, Shimizu T, Nakata T, Kudo T (1999)
Microbiology
145 ( Pt 10) :2813