Difference between revisions of "Part:BBa K808014"
(→Usage and Biology) |
(→Usage and Biology) |
||
Line 9: | Line 9: | ||
<!-- Add more about the biology of this part here--> | <!-- Add more about the biology of this part here--> | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
− | AroY is reported to catalyze the reaction of protocatechuate (3,4-Dihydroxybenzoate) to catechol under anaerobic conditions. This is the last step in the degradation of terephtalic acid to catechol. | + | AroY is reported to catalyze the reaction of protocatechuate (3,4-Dihydroxybenzoate) to catechol under anaerobic conditions. This is the last step in the degradation of terephtalic acid to catechol. Gel permeation chromatography shows that AroY has a homopentomeric structure and a mass of 285.4 kDa (Figure 2). |
[[Image:GPC_AroY.JPG|550px|thumb|left|Figure 2. '''GPC analysis of AroY'''. The Peak of AroY has a retention time of 33 minutes.]] | [[Image:GPC_AroY.JPG|550px|thumb|left|Figure 2. '''GPC analysis of AroY'''. The Peak of AroY has a retention time of 33 minutes.]] |
Revision as of 17:29, 26 September 2012
AroY: Catalyzes protocatechuate to catechol
AroY codes for the protocatechuate deacarboxylase from Klebsiella pneumonie ssp. pneumonie. It has a molecular mass of 57 kDa and is reported to form a complex of five identical AroY subunits. [http://2012.igem.org/Team:TU_Darmstadt/Modeling_GNM#AroY Gaussian network modelling] showed a flexible helix linker. This could be either a membrane anchor or responsible for the formation of a pentamer.
Usage and Biology
AroY is reported to catalyze the reaction of protocatechuate (3,4-Dihydroxybenzoate) to catechol under anaerobic conditions. This is the last step in the degradation of terephtalic acid to catechol. Gel permeation chromatography shows that AroY has a homopentomeric structure and a mass of 285.4 kDa (Figure 2).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 309
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 37
References
- He, Z. and J. Wiegel, Purification and characterization of an oxygen-sensitive, reversible 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum. J Bacteriol, 1996. 178(12): p. 3539-43.
- Grant, D.J. and J.C. Patel, The non-oxidative decarboxylation of p-hydroxybenzoic acid, gentisic acid, protocatechuic acid and gallic acid by Klebsiella aerogenes (Aerobacter aerogenes). Antonie Van Leeuwenhoek, 1969. 35(3): p. 325-43.