5.5.1.1: Muconate cycloisomerase
This is an abbreviated version!
For detailed information about Muconate cycloisomerase, go to the full flat file.
Word Map on EC 5.5.1.1
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5.5.1.1
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muconolactone
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beta-ketoadipate
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cycloisomerization
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protoanemonin
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5-chloromuconolactone
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maleylacetate
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2-chloro-cis,cis-muconate
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cutaneum
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cis-dienelactone
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chlorocatechols
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o-succinylbenzoate
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4-chlorophenol
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5.3.3.4
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3-chloro
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4-chlorocatechol
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gerlt
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phenol-degrading
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ortho-cleavage
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trans-dienelactone
- 5.5.1.1
- muconolactone
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beta-ketoadipate
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cycloisomerization
- protoanemonin
- 5-chloromuconolactone
- maleylacetate
- 2-chloro-cis,cis-muconate
- cutaneum
- cis-dienelactone
- chlorocatechols
- o-succinylbenzoate
- 4-chlorophenol
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5.3.3.4
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3-chloro
- 4-chlorocatechol
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gerlt
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phenol-degrading
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ortho-cleavage
- trans-dienelactone
Reaction
Synonyms
(chloro)-muconate cycloisomerase, (chloro)muconate cycloisomerase, 2-chloromuconate cycloisomerase, ADP1, anti-MLE, CatB, cis,cis-Muconate cycloisomerase, cis,cis-muconate lactonizing enzyme, cis,cis-Muconate-lactonizing enzyme, Enzymes, muconate-lactonizing, Isomerase, muconate cyclo-, MC, MC II, MC O, MCI, MCIase, MCIccaB, MLE, MLE-1, MLE-2, MLEI, muconate cycloisomerase, Muconate cycloisomerase I, Muconate lactonizing enzyme, Rho-2-CMCI, syn-MLE, TcMLE
ECTree
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Crystallization
Crystallization on EC 5.5.1.1 - Muconate cycloisomerase
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in complex with Mg2+, hanging drop vapor diffusion method, using 10% (v/v) 2-propanol, 0.1 M MES, pH 6.0, and 0.2 M Ca(OAc)2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 1.0 M (NH4)2SO4, 0.1 M HEPES, pH 7.0, and 0.5% (w/v) PEG 8000
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in complex with Mg2+, hanging drop vapor diffusion method, using 20% (v/v) PEG 1000, 0.1 M cacodylate, pH 6.5, and 0.2 M MgCl2, or in complex with Mg2+ and cis,cis-muconate, hanging drop vapor diffusion method, using 2.0 M (NH4)2SO4, 0.1 M MES, pH 6.0, and 5% (v/v) isopropanol
hanging drop vapor diffusion method, packing of the octameric enzyme in the crystal form is unusual, because the asymmetric unit contains three subunits
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the crystallographic structure of the chloromuconate cycloisomerase from Rhodococcus opacus is determined at 2.5 A of resolution. Results highlight that a histidine, located in a loop that closes the active site cavity upon the binding of the substrate, could be related to the dehalogenation inability of Rho-2-CMCI
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