Flavin cresol methylhydroxylase

There are five classes of flavin-binding structural folds presented in Table 1 that are identified by the prototype protein in which they were first discovered. These are flavodoxin (FDX), ferredoxin reductase (FNR), triosephosphate isomerase (TIM), glutathione reductase (GR) and p-cresol methylhydroxylase (PCMH). The topologies of four of these five domains are shown in Figure 2. There are also four classes of primary acceptor/donor domain folds that are identified by the prototype protein where they were first discovered. They are cytochrome P450BMP (BMP), cytochrome b5 (CYTB5), cytochrome c (CYTC) and the 2Fe-2S plant-type ferredoxin (FDN). 

FIGURE 8. stereo diagram of p-cresol methylhydroxylase. The flavoprotein subunit is on the left and the cytochrome subunit is on the right. The flavin-binding domain of the flavoprotein subunit is on the bottom and the catalytic domain is on the top. Skeletal models of the heme and FAD prosthetic groups are also shown. 

Bhattacharyya, A., Tollin, G., Mclntire, W. S., and Singer, T. P., 1985, Laser-flash-photolysis studies of p-cresol methylhydroxylase. Electron-transfer properties of the flavin and haem components, Biochem. J. 228 337n345. 

Mclntire, W., Edmondson, D. E., Hopper, D. J., and Singer, T. P., 1981, 8 alpha-(0-tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase. Biochemistry 20 3068n3075. 

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