Agriculture Reference
In-Depth Information
C
A
2+/C
ALMODULIN
-D
EPENDENT
P
ROTEIN
K
INASE
The 72-kDa pea Ca2+/calmodulin-dependent protein kinase activity is
increased in roots at low temperatures and rising salinities. Ca2+
administration raises the kinase level more rapidly than stress application.
Stress upregulation of kinase brought about by low temperatures but not by
salinity is suppressed by EGTA and the calmodulin inhibitor
W7 (Pandey et
al., 2002).
E
NZYME
C
ATALYZING
C
ONJUGATION OF
I
NDOLE
-3-
A
CETIC
A
CID TO
A
SPARTATE
Enzymatic synthesis of indole-3-acetylaspartate (IAA-Asp) by a crude
enzyme preparation from immature pea seeds catalyzing the conjugation of
indole-3-acetic acid to aspartic acids has been reported. IAA-Asp formation is
dependent on ATP and Mg2+, and was linear during a 60 min period. The
optimum pH and optimum temperature of the enzyme are at pH 8.0 and at 30
degrees C, respectively (Ostrowski et al., 2008).
P
-
AMINOBENZOYLGLUTAMATE
H
YDROLASE
p-aminobenzoylglutamate hydrolase activity, which catalyzes the
hydrolysis of p-aminobenzoylglutamate and its polyglutamates to the folate
biosynthesis precursor p-aminobenzoate, was observed in mitochondrial and
cytosol/vacuole fractions of pea leaves (Bozzo et al., 2008).
P
HOSPHOLIPASE
C
D
ELTA
I
SOFORM
The amino acid sequence deduced from the cDNA sequence encoding a
pea phospholipase C-delta exhibits substantial identity to its counterpart other
plants with the typical X, Y and C2 domains. The recombinant product protein
is inactive, despite possession of the requisite amino acids, although the C2
domain is capable of binding calcium. The gene is expressed in all pea tissues,
and is regulated by light in a tissue-specific manner. Expression is higher in
roots than in shoots (Venkataraman et al., 2003).
