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The eukaryotic primase is a heterodimeric enzyme comprising a catalytic subunit Pri1 and a regulatory subunit Pri2.
Enzymes that degrade plant cell wall polysaccharides display a modular architecture comprising a catalytic domain bound to one or more non-catalytic carbohydrate-binding modules (CBMs).
AMPK exists as heterotrimeric complexes comprising a catalytic alpha-subunit and regulatory beta- and gamma-subunits.
PP1 proteins do not exist as free catalytic subunits in the cell but as oligomeric complexes comprising a catalytic structure (PP1c), exerting enzymatic activity, associated with an interacting subunit [2].
PP2As are heterotrimeric complexes comprising a catalytic, structural, and regulatory subunit.
Adenosine monophosphate activated protein kinase is a heterotrimer comprising a catalytic subunit and two regulatory subunits (β and γ).
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The AEP enzymes comprise a catalytic and a non-catalytic subunit.
This complex comprises a catalytic subunit, the integral membrane protein gp91phox and a p22phox subunit.
Calcineurin is a calcium/calmodulin-dependent serine/threonine-specific protein phosphatase that comprises a catalytic A (Cna1) and a regulatory B calcium-binding subunit (Cnb1).
Complex V comprised a catalytic hydrophilic (F1) portion and a hydrophobic (F0) structure that forms the proton channel in the membrane.
CnA comprises a catalytic domain followed by a B subunit regulatory site (Sikkink et al. 1995), a calmodulin binding site (Kincaid et al. 1988) and an inhibitory domain (Hashimoto et al. 1990).
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