| http://purl.uniprot.org/citations/11418568 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11418568 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11418568 | http://www.w3.org/2000/01/rdf-schema#comment | "The genes (caaD1 and caaD2) encoding the trans-3-chloroacrylic acid dehalogenase (CaaD) of the 1,3-dichloropropene-utilizing bacterium Pseudomonas pavonaceae 170 were cloned and heterologously expressed in Escherichia coli and Pseudomonas sp. strain GJ1. CaaD is a protein of 50 kDa that is composed of alpha-subunits of 75 amino acid residues and beta-subunits of 70 residues. It catalyzes the hydrolytic cleavage of the beta-vinylic carbon-chlorine bond in trans-3-chloroacrylic acid with a turnover number of 6.4 s(-1). On the basis of sequence similarity, oligomeric structure, and subunit size, CaaD appears to be related to 4-oxalocrotonate tautomerase (4-OT). This tautomerase consists of six identical subunits of 62 amino acid residues and catalyzes the isomerization of 2-oxo-4-hexene-1,6-dioate, via hydroxymuconate, to yield 2-oxo-3-hexene-1,6-dioate. In view of the oligomeric architecture of 4-OT, a trimer of homodimers, CaaD is postulated to be a hexameric protein that functions as a trimer of alpha beta-dimers. The sequence conservation between CaaD and 4-OT and site-directed mutagenesis experiments suggested that Pro-1 of the beta-subunit and Arg-11 of the alpha-subunit are active-site residues in CaaD. Pro-1 could act as the proton acceptor/donor, and Arg-11 is probably involved in carboxylate binding. Based on these findings, a novel dehalogenation mechanism is proposed for the CaaD-catalyzed reaction which does not involve the formation of a covalent enzyme-substrate intermediate."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.org/dc/terms/identifier | "doi:10.1128/JB.183.14.4269-4277.2001"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.183.14.4269-4277.2001"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Janssen D.B."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Janssen D.B."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Poelarends G.J."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Poelarends G.J."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Saunier R."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/author | "Saunier R."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/name | "J Bacteriol"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/pages | "4269-4277"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/pages | "4269-4277"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/title | "trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/title | "trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase."xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/volume | "183"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://purl.uniprot.org/core/volume | "183"xsd:string |
| http://purl.uniprot.org/citations/11418568 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11418568 |
| http://purl.uniprot.org/citations/11418568 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11418568 |
| http://purl.uniprot.org/citations/11418568 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11418568 |
| http://purl.uniprot.org/citations/11418568 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11418568 |