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. 1998 Sep;64(9):3290–3299. doi: 10.1128/aem.64.9.3290-3299.1998

TABLE 4.

Substrate specificity of the muconate cycloisomerase from A. calcoaceticus” ADP1a

Substrate Km (μM) kcat (min−1) kcat/Km (min−1 μM−1)
cis,cis-Muconate 130 ± 10 3,700 ± 200 29
2-Chloro-cis,cis-muconate 290 ± 90 17 ± 4 0.06
3-Chloro-cis,cis-muconate (<10)b
2,4-Dichloro-cis,cis-muconate (<10)b
3-Fluoro-cis,cis-muconate 100 ± 10 2,600 ± 200 24
2-Methyl-cis,cis-muconate 490 ± 120 4,700 ± 1,000 9.7
3-Methyl-cis,cis-muconate 99 ± 7 1,800 ± 100 18
a

The Km and kcat values were determined as described in Materials and Methods. Standard deviations were calculated with the Enzfitter program. The measurements were determined with an enzyme preparation described previously (57). 

b

The activity at a substrate concentration of 0.1 mM was below the detection limit for this measurement. Consequently, kcat, Km, and kcat/Km values could not be determined.