EC Number   |
General Information |
Reference |
|---|
    3.8.1.8 | evolution |
both enzyme AtzA and the alternative chlorohydrolase TrzN from Arthrobacter aurescens belong to the same large family of amidohydrolases, although they are so different physically and phylogenetically that it is likely that atrazine chlorohydrolase activity evolved independently in each enzyme, comparison of enzyme features, overview. In contrast to most other known hydrolytic dehalogenases, which use an active-site carboxylic acid (Asp) to displace the halide ion, the metal-dependent reaction mechanisms of AtzA and TrzN make these two enzyme lineages somewhat unusual in nature |
733014 |
| 3.8.1.8 | evolution |
TrzN uniquely positions threonine 325 in place of a conserved aspartate that ligates the metal in most mononuclear amidohydrolases superfamily members |
-, 719887 |
| 3.8.1.8 | metabolism |
the enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP |
733014 |
| 3.8.1.8 | metabolism |
the enzyme is critical in the atrazine degradation pathway |
735319 |
| 3.8.1.8 | more |
development of fiber-optic biosensors for detection of atrazine using the atrazine chlorohydrolase, quantification of hydrochloric acid release, optimization, overview |
-, 718576 |
| 3.8.1.8 | more |
enzyme active site structure, overview. The channel, substrate-binding pocket and active site are comprised of His66, His68, Gln71, Phe84, Tyr85, Trp87, Leu88, Phe89, Val92, Tyr93, Asp128, Met155, Phe157, Met160, Asp161, Ile164, Gln165, Val168, Leu180, Ser182, Ile183, Met184, Ala216, Thr217, Thr219, Ala220, His243, Glu246, Asp250, His276, Leu305, Asp327, Asn328 and Ser331. Structure comparison of AtzA and the alternative chlorohydrolase TrzN from Arthrobacter aurescens, overview |
733014 |
| 3.8.1.8 | more |
homology model of the AtzA wild-type enzyme and mutant enzymes. Only five of the seven substitutions (V92L, M155V, M256I, Y261S and A296T) can be accurately located using the homology model, the remaining two (A170T and P258T) lying in regions of primary structure that can not be accurately mapped to the template used in the model (a protein of unknown function from Thermotoga maritima; PDB: 1J6P) |
733440 |
| 3.8.1.8 | more |
homology modeling of enzyme AtzA, structure modeling and distribution of substitution sites |
733315 |
| 3.8.1.8 | physiological function |
atrazine chlorohydrolase 2 initiates bacterial metabolism of the herbicide atrazine by hydrolytic displacement of a chlorine substituent from the s-triazine ring |
-, 719887 |
| 3.8.1.8 | physiological function |
Pseudomonas sp. strain ADP completely biodegrades atrazine to carbon dioxide and ammonia through the consecutive action of six catabolic enzymes, encoded by atzABCDEF, located on a selftransmissible plasmid, pADP-1. The first reaction is initiated by the enzyme AtzA, resulting in the dechlorination of atrazine to yield hydroxyatrazine, which is non-herbicidal and non-phytotoxic |
735319 |
