Difference between revisions of "Part:BBa K5175007"

Revision as of 23:58, 1 October 2024

tphA3 TPA 1,2-dioxygenase (TPADO) is a two-component oxygenase consisting of three parts, TphA1, TphA2, and TphA3, which together enable TPADO to effectively catalyze the oxidative reaction of TPA, converting TPA to the intermediate product 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). TphB is a dehydrogenase that oxidizes the diol moiety (two hydroxyl groups) of DCD to a keto group, resulting in the production of PCA.TphA2, TphA3 constitute the large and small subunits of the TPADO oxidase component responsible for binding to the TPA substrate and catalyzing the oxygenation reaction in the active site.TphA2 contains the active site in direct contact with the substrate, TPA, and contains the Cys-X1-His X17-Cys-X2-His pattern, binds to Rieske-type [2Fe-2S] iron-sulfur clusters and participates in electron transfer, which is a key part of the catalytic reaction of dioxygenases , TphA3 participates in the construction of the substrate channel or the appropriate positioning of the active site, and assists TphA2 in completing the oxidation reaction; TphA1 does not directly participate in the oxygenation reaction, but it contains a [2Fe -2S] iron-sulfur cluster and a flavin adenine dinucleotide (FAD) binding site that transfers electrons from an electron donor (e.g., NADPH) to the oxidized component of TPADO.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 148
1000
COMPATIBLE WITH RFC[1000]

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 __NOTOC__
 <partinfo>BBa_K5175007 short</partinfo>
+TPA 1,2-dioxygenase (TPADO) is a two-component oxygenase consisting of three parts, TphA1, TphA2, and TphA3, which together enable TPADO to effectively catalyze the oxidative reaction of TPA, converting TPA to the intermediate product 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). TphB is a dehydrogenase that oxidizes the diol moiety (two hydroxyl groups) of DCD to a keto group, resulting in the production of PCA.TphA2, TphA3 constitute the large and small subunits of the TPADO oxidase component responsible for binding to the TPA substrate and catalyzing the oxygenation reaction in the active site.TphA2 contains the active site in direct contact with the substrate, TPA, and contains the Cys-X1-His X17-Cys-X2-His pattern, binds to Rieske-type [2Fe-2S] iron-sulfur clusters and participates in electron transfer, which is a key part of the catalytic reaction of dioxygenases , TphA3 participates in the construction of the substrate channel or the appropriate positioning of the active site, and assists TphA2 in completing the oxidation reaction; TphA1 does not directly participate in the oxygenation reaction, but it contains a [2Fe -2S] iron-sulfur cluster and a flavin adenine dinucleotide (FAD) binding site that transfers electrons from an electron donor (e.g., NADPH) to the oxidized component of TPADO.
 <!-- Add more about the biology of this part here
 ===Usage and Biology===
-TPA 1,2-dioxygenase (TPADO) is a two-component oxygenase consisting of three parts, TphA1, TphA2, and TphA3, which together enable TPADO to effectively catalyze the oxidative reaction of TPA, converting TPA to the intermediate product 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). TphB is a dehydrogenase that oxidizes the diol moiety (two hydroxyl groups) of DCD to a keto group, resulting in the production of PCA.TphA2, TphA3 constitute the large and small subunits of the TPADO oxidase component responsible for binding to the TPA substrate and catalyzing the oxygenation reaction in the active site.TphA2 contains the active site in direct contact with the substrate, TPA, and contains the Cys-X1-His X17-Cys-X2-His pattern, binds to Rieske-type [2Fe-2S] iron-sulfur clusters and participates in electron transfer, which is a key part of the catalytic reaction of dioxygenases , TphA3 participates in the construction of the substrate channel or the appropriate positioning of the active site, and assists TphA2 in completing the oxidation reaction; TphA1 does not directly participate in the oxygenation reaction, but it contains a [2Fe -2S] iron-sulfur cluster and a flavin adenine dinucleotide (FAD) binding site that transfers electrons from an electron donor (e.g., NADPH) to the oxidized component of TPADO.
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