| http://purl.uniprot.org/citations/12520360 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12520360 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12520360 | http://www.w3.org/2000/01/rdf-schema#comment | "The first cloning and characterization of the gene katA, encoding the major catalase (KatA), from Xanthomonas is reported. A reverse genetic approach using a synthesized katA-specific DNA probe to screen a X. campestris pv. phaseoli genomic library was employed. A positively hybridizing clone designated pKat29 that contained a full-length katA was isolated. Analysis of the nucleotide sequence revealed an open reading frame of 1,521 bp encoding a 507-amino acid protein with a theoretical molecular mass of 56 kDa. The deduced amino acid sequence of KatA revealed 84% and 78% identity to CatF of Pseudomonas syringae and KatB of P. aeruginosa, respectively. Phylogenetic analysis places Xanthomonas katA in the clade I group of bacterial catalases. Unexpectedly, expression of katA in a heterologous Escherichia coli host resulted in a temperature-sensitive expression. The KatA enzyme was purified from an overproducing mutant of X. campestris and was characterized. It has apparent K(m) and V(max) values of 75 m M [H(2)O(2)] and 2.55 x 10(5) micromol H(2)O(2) micromol heme(-1) s(-1), respectively. The enzyme is highly sensitive to 3-amino-1,2,4-triazole and NaN(3), has a narrower optimal pH range than other catalases, and is more sensitive to heat inactivation."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.org/dc/terms/identifier | "doi:10.1007/s00284-002-3812-8"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.org/dc/terms/identifier | "doi:10.1007/s00284-002-3812-8"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Mongkolsuk S."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Mongkolsuk S."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Loewen P.C."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Loewen P.C."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Switala J."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Switala J."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Vattanaviboon P."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Vattanaviboon P."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Chauvatcharin N."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/author | "Chauvatcharin N."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/name | "Curr. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/name | "Curr Microbiol"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/pages | "83-87"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/pages | "83-87"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/title | "Cloning and characterization of katA, encoding the major monofunctional catalase from Xanthomonas campestris pv. phaseoli and characterization of the encoded catalase KatA."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/title | "Cloning and characterization of katA, encoding the major monofunctional catalase from Xanthomonas campestris pv. phaseoli and characterization of the encoded catalase KatA."xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/volume | "46"xsd:string |
| http://purl.uniprot.org/citations/12520360 | http://purl.uniprot.org/core/volume | "46"xsd:string |