home
***
CD-ROM
|
disk
|
FTP
|
other
***
search
/
Danny Amor's Online Library
/
Danny Amor's Online Library - Volume 1.iso
/
bbs
/
misc
/
prosite.lha
/
DATA
/
PDOC00403
< prev
next >
Wrap
Text File
|
1995-07-26
|
2KB
|
34 lines
***********************************************
* Chalcone and stilbene synthases active site *
***********************************************
Chalcone synthases (CHS) (EC 2.3.1.74) and stilbene synthases (STS) (formerly
known as resveratrol synthases) are related plant enzymes [1]. CHS is an
important enzyme in flavanoid biosynthesis and STS a key enzyme in stilbene-
type phyloalexin biosynthesis. Both enzymes catalyze the addition of three
molecules of malonyl-CoA to a starter CoA ester (a typical example is
4-coumaroyl-CoA), producing either a chalcone (with CHS) or stilbene (with
STS).
These enzymes are proteins of about 390 amino-acid residues. A conserved
cysteine residue, located in the central section of these proteins, has been
shown [2] to be essential for the catalytic activity of both enzymes and
probably represents the binding site for the 4-coumaryl-CoA group. The region
around this active site residue is well conserved and can be used as a
signature pattern.
-Consensus pattern: G-C-[FY]-[GA]-G-G-T-x(2)-R
[C is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Expert(s) to contact by email: Schroeder J.
raf@sun1.ruf.uni-freiburg.de
-Last update: June 1992 / Pattern and text revised.
[ 1] Schroeder J., Schroeder G.
Z. Naturforsch. 45C:1-8(1990).
[ 2] Lanz T., Tropf S., Marner F.-J., Schroeder J., Schroeder G.
J. Biol. Chem. 266:9971-9976(1991).