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Your query returned 10 entries. Printable version
EC | 3.5.1.54 | ||||||||||||||
Accepted name: | allophanate hydrolase | ||||||||||||||
Reaction: | urea-1-carboxylate + H2O = 2 CO2 + 2 NH3 | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | allophanate = urea-1-carboxylate | ||||||||||||||
Other name(s): | allophanate lyase; AtzF; TrzF | ||||||||||||||
Systematic name: | urea-1-carboxylate amidohydrolase | ||||||||||||||
Comments: | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6]. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-72-6 | ||||||||||||||
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EC | 3.5.1.84 | ||||||||||||||
Accepted name: | biuret amidohydrolase | ||||||||||||||
Reaction: | biuret + H2O = urea-1-carboxylate + NH3 | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | biuret = imidodicarbonic diamide allophanate = urea-1-carboxylate |
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Other name(s): | biuH (gene name) | ||||||||||||||
Systematic name: | biuret amidohydrolase | ||||||||||||||
Comments: | The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95567-88-7 | ||||||||||||||
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EC | 3.5.1.131 | ||||||||||||||
Accepted name: | 1-carboxybiuret hydrolase | ||||||||||||||
Reaction: | 1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3 | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | carboxybiuret = carbamoylcarbamoylcarbamic acid | ||||||||||||||
Other name(s): | atzEG (gene names) | ||||||||||||||
Systematic name: | 1-carboxybiuret amidohydrolase | ||||||||||||||
Comments: | The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
References: |
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EC | 3.5.2.15 | ||||||||||||||
Accepted name: | cyanuric acid amidohydrolase | ||||||||||||||
Reaction: | cyanuric acid + H2O = 1-carboxybiuret | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine 1-carboxybiuret = N-[(carbamoylamino)carbonyl]carbamate |
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Other name(s): | atzD (gene name); trzD (gene name) | ||||||||||||||
Systematic name: | cyanuric acid amidohydrolase | ||||||||||||||
Comments: | The enzyme catalyses the ring cleavage of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is highly specific for cyanuric acid. The product was initially thought to be biuret, but was later shown to be 1-carboxybiuret. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 132965-78-7 | ||||||||||||||
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EC | 3.5.4.42 | ||||||||||||||
Accepted name: | N-isopropylammelide isopropylaminohydrolase | ||||||||||||||
Reaction: | N-isopropylammelide + H2O = cyanuric acid + isopropylamine | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | N-isopropylammelide = 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine cyanuric acid = s-triazine-2,4,6-triol |
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Other name(s): | atzC (gene name) | ||||||||||||||
Systematic name: | N-isopropylammelide isopropylaminohydrolase | ||||||||||||||
Comments: | Requires Zn2+. This bacterial enzyme is involved in degradation of the herbicide atrazine. It can hydrolyse other N-substituted amino dihydroxy-s-triazine molecules, and prefers substrates with linear N-alkyl groups to those with branched alkyl groups. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 203810-02-0 | ||||||||||||||
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EC | 3.5.4.43 | ||||||||||||||
Accepted name: | hydroxydechloroatrazine ethylaminohydrolase | ||||||||||||||
Reaction: | hydroxyatrazine + H2O = N-isopropylammelide + ethylamine | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | hydroxyatrazine = 4-(ethylamino)-6-(isopropylamino)-1,3,5-triazin-2-ol N-isopropylammelide = 6-(isopropylamino)-1,3,5-triazine-2,4-diol |
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Other name(s): | atzB (gene name); 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase | ||||||||||||||
Systematic name: | hydroxyatrazine ethylaminohydrolase | ||||||||||||||
Comments: | Contains Zn2+. This bacterial enzyme is involved in degradation of the herbicide atrazine. The enzyme has a broad substrate range, and requires a monohydroxylated s-triazine ring with a minimum of one primary or secondary amine substituent and either a chloride or amine leaving group. It catalyses both deamination and dechlorination reactions. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
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EC | 3.5.4.45 | ||||||||||||||
Accepted name: | melamine deaminase | ||||||||||||||
Reaction: | (1) melamine + H2O = ammeline + NH3 (2) ammeline + H2O = ammelide + NH3 |
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Glossary: | melamine = 2,4,6-triamino-1,3,5-triazine ammeline = 4,6-diamino-1,3,5-triazin-2-ol ammelide = 6-amino-1,3,5-triazine-2,4-diol |
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Other name(s): | triA (gene name) | ||||||||||||||
Systematic name: | melamine aminohydrolase | ||||||||||||||
Comments: | The enzyme, isolated from the bacterium Acidovorax citrulli, performs the deamination of melamine 15-fold faster than the deamination of ammeline. It also has activity with 2-chloro-4,6-diamino-s-triazine, but has no activity toward halo-substituted triazine ring compounds such as atrazine (cf. EC 3.8.1.8, atrazine chlorohydrolase). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 3.5.99.3 | ||||||||||||||
Transferred entry: | hydroxydechloroatrazine ethylaminohydrolase. Now EC 3.5.4.43, hydroxydechloroatrazine ethylaminohydrolase | ||||||||||||||
EC | 3.5.99.4 | ||||||||||||||
Transferred entry: | N-isopropylammelide isopropylaminohydrolase. Now EC 3.5.4.42, N-isopropylammelide isopropylaminohydrolase | ||||||||||||||
EC | 3.8.1.8 | ||||||||||||||
Accepted name: | atrazine chlorohydrolase | ||||||||||||||
Reaction: | atrazine + H2O = hydroxyatrazine + chloride | ||||||||||||||
For diagram of atrazine catabolism, click here | |||||||||||||||
Glossary: | atrazine = 6-chloro-N-ethyl-N′-isopropyl-1,3,5-triazine-2,4-diamine hydroxyatrazine = 4-(ethylamino)-6-(isopropylamino)-1,3,5-triazin-2-ol |
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Other name(s): | AtzA | ||||||||||||||
Systematic name: | atrazine chlorohydrolase | ||||||||||||||
Comments: | Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 168680-16-8 | ||||||||||||||
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