Modulation of phosphoenolpyruvate carboxylase phosphorylation in leaves of Amaranthus hypochondriacus, a NAD-ME Type of C4 plant

Title:

Modulation of phosphoenolpyruvate carboxylase phosphorylation in leaves of Amaranthus hypochondriacus, a NAD-ME Type of C4 plant

Creator:

Parvathi, K., Gayathri, J., Maralihalli, G. B., Bhagwat, A. S., and Raghavendra, A. S.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:09a5a3b5-0b87-4d67-a656-825b6c2fc188
uuid:09a5a3b5-0b87-4d67-a656-825b6c2fc188
issn:0300-3604
doi:10.1023/A:1026783521733

Subject:

calcium, calcium-dependent protein kinase, and PEPC-protein kinase

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

PEP carboxylase (PEPC) in leaves of C4 plants is activated by phosphorylation of enzyme by a PEPC-protein kinase (PEPC-PK). We reevaluated the pattern of PEPC phosphorylation in leaf extracts of Amaranthus hypochondriacus. It was dependent on Ca2+, the optimum concentration of which for stimulation was 10 mM. The extent of stimulation was inhibited by 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid (BAPTA), a Ca2+ chelator. The inhibition by BAPTA was relieved by the addition of Ca2+ but not by the addition of Mg2+. The stimulation by Ca2+ of PEPC phosphorylation was marginally enhanced by calmodulin (CaM), but not by diacylglycerol (DAG). Phosphorylation was strongly restricted by Ca2+ or Ca2+-CaM-dependent protein kinase inhibitors. Thus phosphorylation of PEPC is Ca2+-dependent in leaves of A. hypochondriacus and a calcium-dependent protein kinase (CDPK) may modulate PEPC-PK and subsequently the phosphorylation status of PEPC. and K. Parvathi ... [et al.].

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

23-28

Source:

Photosynthetica | 2000 Volume:38 | Number:1

Harvested from:

CDK

Metadata only:

false