View source for DTDP-L-rhamnose 4-epimerase

{{Infobox enzyme
| Name = 2-hydroxymuconate tautomerase
| EC_number = 5.3.2.6
| CAS_number = 
| IUBMB_EC_number = 5/3/2/6
| GO_code = 
| image = 
| width = 
| caption =
}}
'''2-hydroxymuconate tautomerase''' ({{EC number|5.3.2.6}}, ''4-oxalocrotonate tautomerase'', ''4-oxalocrotonate isomerase'', ''cnbG (gene)'', ''praC (gene)'', ''xylH (gene)'') is an [[enzyme]] with system name ''(2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase''.<ref>{{cite journal | title = Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol |author = Whitman, C.P., Aird, B.A., Gillespie, W.R. and Stolowich, N.J. |journal = J. Am. Chem. Soc. |year = 1991 |volume = 113 |pages = 3154–3162 |pmid = }}</ref><ref>{{cite journal | title = Stereospecific ketonization of 2-hydroxymuconate by 4-oxalocrotonate tautomerase and 5-(carboxymethyl)-2-hydroxymuconate isomerase |author = Whitman, C.P., Hajipour, G., Watson, R.J., Johnson, W.H., Jr., Bembenek, M.E. and Stolowich, N.J. |journal = J. Am. Chem. Soc. |year = 1992 |volume = 114 |pages = 10104–10110 |pmid = }}</ref><ref>{{cite journal | title = Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases |author = Subramanya, H.S., Roper, D.I., Dauter, Z., Dodson, E.J., Davies, G.J., Wilson, K.S. and Wigley, D.B. |journal = Biochemistry |year = 1996 |volume = 35 |pages = 792–802 |pmid = 8547259 |doi=10.1021/bi951732k |issue=3}}</ref><ref>{{cite journal | title = Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies |author = Stivers, J.T., Abeygunawardana, C., Mildvan, A.S., Hajipour, G., Whitman, C.P. and Chen, L.H. |journal = Biochemistry |year = 1996 |volume = 35 |pages = 803–813 |pmid = 8547260 |doi=10.1021/bi951077g |issue=3}}</ref><ref>{{cite journal | title = Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in <em>Bacillus subtilis</em>: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions |author = Wang, S.C., Johnson, W.H., Jr., Czerwinski, R.M., Stamps, S.L. and Whitman, C.P. |journal = Biochemistry |year = 2007 |volume = 46 |pages = 11919–11929 |pmid = 17902707 |doi=10.1021/bi701231a |issue=42}}</ref><ref>{{cite journal | title = Uncovering the protocatechuate 2,3-cleavage pathway genes |author = Kasai, D., Fujinami, T., Abe, T., Mase, K., Katayama, Y., Fukuda, M. and Masai, E. |journal = J. Bacteriol. |year = 2009 |volume = 191 |pages = 6758–6768 |pmid = 19717587 |doi=10.1128/JB.00840-09 |pmc=2795304}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate <math>\rightleftharpoons</math> (3E)-2-oxohex-3-enedioate

Involved in the meta-cleavage pathway for the degradation of [[phenol]]s, modified phenols and [[catechol]]s. 


== References ==
{{reflist}}

== External links ==
* {{MeshName|2-hydroxymuconate+tautomerase}}

[[Category:EC 5.3.2]]