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Titolo:
Molecular characterization of the genes pcaG and pcaH, encoding protocatechuate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR199
Autore:
Overhage, J; Kresse, AU; Priefert, H; Sommer, H; Krammer, G; Rabenhorst, J; Steinbuchel, A;
Indirizzi:
Univ Munster, Inst Mikrobiol, D-48149 Munster, Germany Univ Munster Munster Germany D-48149 Mikrobiol, D-48149 Munster, Germany GBF Natl Res Ctr Biotechnol, D-38124 Braunschweig, Germany GBF Natl Res Ctr Biotechnol Braunschweig Germany D-38124 chweig, Germany Haarmann & Reimer GMBH, Corp Res, D-37601 Holzminden, Germany Haarmann & Reimer GMBH Holzminden Germany D-37601 01 Holzminden, Germany
Titolo Testata:
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
fascicolo: 3, volume: 65, anno: 1999,
pagine: 951 - 960
SICI:
0099-2240(199903)65:3<951:MCOTGP>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
P-HYDROXYBENZOATE HYDROXYLASE; 3-CARBOXY-CIS,CIS-MUCONATE LACTONIZING ENZYME; ESCHERICHIA-COLI; ACINETOBACTER-CALCOACETICUS; ALCALIGENES-EUTROPHUS; AGROBACTERIUM-TUMEFACIENS; EVOLUTIONARY DIVERGENCE; STRUCTURAL GENE; IDENTIFICATION; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Priefert, H Univ Munster, Inst Mikrobiol, Corrensstr 3, D-48149 Munster, Germany Univ Munster Corrensstr 3 Munster Germany D-48149 er, Germany
Citazione:
J. Overhage et al., "Molecular characterization of the genes pcaG and pcaH, encoding protocatechuate 3,4-dioxygenase, which are essential for vanillin catabolism in Pseudomonas sp. strain HR199", APPL ENVIR, 65(3), 1999, pp. 951-960

Abstract

Pseudomonas sp, strain HR199 is able to utilize eugenol (4-allyl-2-methoxyphenol), vanillin (4-hydroxy-3-methoxybenzaldehyde), or protocatechuate as the sole carbon source for growth. Mutants of this strain which were impaired in the catabolism of vanillin but retained the ability to utilize eugenol or protocatechuate were obtained after nitrosoguanidine mutagenesis, One mutant (SK6169) was used as recipient of a Pseudomonas sp, strain HR199 genomic library in cosmid pVK100, and phenotypic complementation was achieved with a 5.8-kbp EcoRI fragment (E58), The amino acid sequences deduced from two corresponding open reading frames (ORF) identified on E58 revealed highdegrees of homology to pcaG and pcaH, encoding the two subunits of protocatechuate 3,4-dioxygenase. Three additional ORF most probably encoded a 4-hydroxybenzoate 3-hydroxylase (PobA) and two putative regulatory proteins, which exhibited homology to PcaQ of Agrobacterium tumefaciens and PobR of Pseudomonas aeruginosa, respectively. Since mutant SK6169 was also complemented by a subfragment of E58 that harbored only pcaH, this mutant was most probably lacking a functional beta subunit of the protocatechuate 3,4-dioxygenase. Since this mutant was still able to grow on protocatechuate and lackedprotocatechuate 4,5-dioxygenase and protocatechuate 2,3-dioxygenase, the degradation had to be catalyzed by different enzymes. Two other mutants (SK6184 and SK6190), which were also impaired in the catabolism of vanillin, were not complemented by fragment E58, Since these mutants accumulated 3-carboxy muconolactone during cultivation on eugenol, they most probably exhibited a defect in a step of the catabolic pathway following the ortho cleavage. Moreover, in these mutants cyclization of 3-carboxymuconic acid seems to occur by a syn absolute stereochemical course, which is normally only observed for cis,cis-muconate lactonization in pseudomonads. In conclusion, vanillin is degraded through the ortho-cleavage pathway in Pseudomonas sp, strain HR199 whereas protocatechuate could also be metabolized via a different pathway in the mutants.

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Documento generato il 03/04/20 alle ore 04:26:57