Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1NQXDK (E)-5-(dihydroxymethylidene)- 2-oxo-hept-3...

Synonyms:

Bendrat, K. et al., Hermanowski-Vosatka, A. et al., Soares, T.A. et al., Nishihira, J., Alonso, J.M. et al., et al.

Hermanowski-Vosatka, Mundt, Ayala, Goyal, Hanlon, Czerwinski, Wright, Whitman,

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Disease relevance of C04186

Preliminary crystallographic analysis of 5-carboxymethyl-2-hydroxymuconate isomerase from Escherichia coli [1].

High impact information on C04186

The three-dimensional structure of MIF is strikingly similar to that of two microbial enzymes (4-oxalocrotonate tautomerase and 5-carboxymethyl-2-hydroxymuconate isomerase) that otherwise share little sequence identity with MIF [2].
MIF also has been described recently to exhibit dopachrome tautomerase activity and to be structurally homologous to the bacterial enzymes 4-oxalocrotonate tautomerase (4-OT) and 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) [3].
This architecture is almost identical to 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) and is related to the E. coli signal transducing protein PII [4].
Purification, some properties and nucleotide sequence of 5-carboxymethyl-2-hydroxymuconate isomerase of Escherichia coli C [5].
Kinetic properties of purified 5-carboxymethyl-2-hydroxymuconate semialdehyde (CHMSA) dehydrogenase (EC 1.2.1.-) in the 4-hydroxyphenylacetate meta-cleavage pathway from Escherichia coli have been studied [6].

Biological context of C04186

Although considered a cytokine, MIF possesses a three-dimensional structure and active site similar to those of 4-oxalocrotonate tautomerase and 5-carboxymethyl-2-hydroxymuconate isomerase [7].

Associations of C04186 with other chemical compounds

We report the results of molecular docking simulations of 4-oxalocrotonate tautomerase with two substrates, 2-hydroxymuconate and 5-carboxymethyl-2-hydroxymuconate. pKa calculations are also performed for the free enzyme [8].

Gene context of C04186

These tertiary structures showed that this protein forms a homotrimer with each monomer consisting of two beta/alpha/beta motifs, thus resembling 5-carboxymethyl-2-hydroxymuconate isomerase and d-dopachrome tautomerase [9].

References

Preliminary crystallographic analysis of 5-carboxymethyl-2-hydroxymuconate isomerase from Escherichia coli. Wigley, D.B., Roper, D.I., Cooper, R.A. J. Mol. Biol. (1989) [Pubmed]
Enzymatically inactive macrophage migration inhibitory factor inhibits monocyte chemotaxis and random migration. Hermanowski-Vosatka, A., Mundt, S.S., Ayala, J.M., Goyal, S., Hanlon, W.A., Czerwinski, R.M., Wright, S.D., Whitman, C.P. Biochemistry (1999) [Pubmed]
Biochemical and mutational investigations of the enzymatic activity of macrophage migration inhibitory factor. Bendrat, K., Al-Abed, Y., Callaway, D.J., Peng, T., Calandra, T., Metz, C.N., Bucala, R. Biochemistry (1997) [Pubmed]
Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1 A resolution. Sugimoto, H., Suzuki, M., Nakagawa, A., Tanaka, I., Nishihira, J. FEBS Lett. (1996) [Pubmed]
Purification, some properties and nucleotide sequence of 5-carboxymethyl-2-hydroxymuconate isomerase of Escherichia coli C. Roper, D.I., Cooper, R.A. FEBS Lett. (1990) [Pubmed]
Kinetic properties of 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase from Escherichia coli. Alonso, J.M., Garrido-Pertierra, A. Biochimie (1986) [Pubmed]
Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity. Lubetsky, J.B., Swope, M., Dealwis, C., Blake, P., Lolis, E. Biochemistry (1999) [Pubmed]
Docking of 4-oxalocrotonate tautomerase substrates: implications for the catalytic mechanism. Soares, T.A., Goodsell, D.S., Briggs, J.M., Ferreira, R., Olson, A.J. Biopolymers (1999) [Pubmed]
Novel pathophysiological aspects of macrophage migration inhibitory factor (review). Nishihira, J. Int. J. Mol. Med. (1998) [Pubmed]

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