TABLE 1

Molecular interactions between each tetrapeptide (CNHT, CRVI, CFNL, KARC, RAQC, and DALC) and active site residues of mushroom tyrosinase

The numbers 1, 2, 3, 4, 5, and 6 in this table stand for electrostatic interactions, hydrogen bonding, and hydrophobic π-π, cation-π, and anion-π interactions, respectively. The N terminus NH₂, amide, side chain, and C-terminal carboxyl groups of tetrapeptides are abbreviated as n, a, s, and c, respectively.

	Glu189				Ala246				Val248				Glu256				Asn260				Phe264				Arg268				Met280				Gly281				Ser282				Val283				Pro284				Glu322
	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c	n	a	s	c
CNHT
C
n																1				2
s
a
N
s																																																					2
a
H
s												3
a																				2
T
s
c																												1
CRVI
C
n																1				2
s
a
R
s							2																																													1
a
V
s												3												3
a
I
s																																												3				3
c																												1
CFNL
C
n																1				2
s
a
F
s												3																																								6
a
N
s																																			2
a
L
s																																												3				3
c																												1
KARC
K
n
s				1
a																																								2
A
s
a
R
s							2																																													1
a
C
s
c																				2
RAQC
R
n
s				1
a																																								2
A
s																								3
a
Q
s																																																				2
a
C
s
c																				2
DALC
D
n
s
a																																								2
A
s																								3
a
L
s												3												3
a
C
s
c																				2