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{PDOC00424}
{PS00488; PAL_HISTIDASE}
{BEGIN}
**********************************************************
* Phenylalanine and histidine ammonia-lyases active site *
**********************************************************
Phenylalanine ammonia-lyase (EC 4.3.1.5) (PAL) is a key enzyme of plant and
fungi phenylpropanoid metabolism which is involved in the biosynthesis of a
wide variety of secondary metabolites such as flavanoids, furanocoumarin
phytoalexins and cell wall components. These compounds have many important
roles in plants during normal growth and in responses to environmental stress.
PAL catalyzes the removal of an ammonia group from phenylalanine to form
trans-cinnamate.
Histidine ammonia-lyase (EC 4.3.1.3) (histidase) catalyzes the first step in
histidine degradation, the removal of an ammonia group from histidine to
produce urocanic acid.
The two types of enzymes are functionally and structurally related [1]. They
are the only enzymes which are known to have the modified amino acid dehydro-
alanine (DHA) in their active site. A serine residue has been shown [2,3,4] to
be the precursor of this essential electrophilic moiety. The region around
this active site residue is well conserved and can be used as a signature
pattern.
-Consensus pattern: [GS]-[STG]-[LIVM]-[STG]-[SAC]-S-G-[DH]-L-x-[PN]-L-[SA]-
x(2,3)-[SAGVTL]
[S 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.
-Last update: April 2006 / Pattern revised.
[ 1] Taylor R.G., Lambert M.A., Sexsmith E., Sadler S.J., Ray P.N.,
Mahuran D.J., McInnes R.R.
"Cloning and expression of rat histidase. Homology to two bacterial
histidases and four phenylalanine ammonia-lyases."
J. Biol. Chem. 265:18192-18199(1990).
PubMed=2120224
[ 2] Langer M., Reck G., Reed J., Retey J.
"Identification of serine-143 as the most likely precursor of
dehydroalanine in the active site of histidine ammonia-lyase. A study
of the overexpressed enzyme by site-directed mutagenesis."
Biochemistry 33:6462-6467(1994).
PubMed=8204579
[ 3] Schuster B., Retey J.
"Serine-202 is the putative precursor of the active site
dehydroalanine of phenylalanine ammonia lyase. Site-directed
mutagenesis studies on the enzyme from parsley (Petroselinum crispum
L.)."
FEBS Lett. 349:252-254(1994).
PubMed=8050576
[ 4] Taylor R.G., McInnes R.R.
"Site-directed mutagenesis of conserved serines in rat histidase.
Identification of serine 254 as an essential active site residue."
J. Biol. Chem. 269:27473-27477(1994).
PubMed=7961661
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{END}
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