Cloning, expression, and characterization of the katG gene, encoding catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading bacterium Mycobacterium sp. strain PYR-1

Article Abstract:

Research describes the construction of an oligonucleotide probe that contains part of the gene encoding catalase-peroxidase to screen the genomic library of Mycobacterium sp. strain PYR-1. Data show that the enzyme is involved in the polycylic aromatic hydrocarbon metabolism of the bacterium as indicated by its induction in pyrene-containing cultures.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

Molecular cloning, nucleotide sequence, and expression of genes encoding a polycyclic aromatic ring dioxygenase from Mycobacterium sp. strain PYR-1

Article Abstract:

Three genes from Mycobacterium sp. strain PYR-1 encoding a dioxygenase were subcloned and expressed in Escherichia coli using the pBAD/ThioFusion system. This enzyme is involved in degrading polycyclic hydrocarbons.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code:

Purification of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Pseudomonas putida OU83 and characterization of the gene (bphC)

Article Abstract:

The bphC gene from Pseudomonas putida OU83's PCB pathway is cloned and sequenced to apparent homogeneity. The gene product is then purified and compared with the 2,3-dihydroxybiphenyl 1,2-dioxygenase (2,3-DBPD) proteins from the rest of the bphC gene family. Results show that 2,3-DBPD is an octamer of identical subunits. The data also suggest that its protein sequence consists of 292 amino acid residues with a calculated molecular mass of 31.9 kDa.

User Contributions:

Comment about this article or add new information about this topic:

Comment:  (50-4000 characters)

Name:

E-mail:

Security Code: