Sequence and structural features of plant and fungal tyrosinases.
Tyrosinases from various organisms are compared with respect to enzymatic structure, primary, secondary and tertiary structure, domain structure, Cu binding sites, maturation mechanism and activation mechanism. On the basis of these comparisons, and by using hemocyanin structure as a template, a structure model for the active site of tyrosinases is proposed.
van Gelder
C W
CW
Agrotechnological Research Institute (ATO-DLO), Wageningen, The Netherlands.
Flurkey
W H
WH
Wichers
H J
HJ
D000595:Amino Acid Sequence; D000818:Animals; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D005656:Fungal Proteins; D010940:Plant Proteins; D014442:Monophenol Monooxygenase