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Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain is located at the C-Terminus end of the kinase. On the other side of the kinase at the N-Terminus end, sits the actin-binding domain, which allows MYLK to form interactions with actin filaments, keeping it in place. [4] [5]
This gene, a muscle member of the immunoglobulin superfamily, encodes a myosin light-chain kinase, which is a calcium-/calmodulin-dependent enzyme.This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity.
Their experiment proved the existence of a photosynthetic unit. Gaffron and Wohl later interpreted the experiment and realized that the light absorbed by the photosynthetic unit was transferred. [7] This reaction occurs at the reaction center of Photosystem II and takes place in cyanobacteria, algae and green plants. [8]
The structure and function of cytochrome b 6 f (in chloroplasts) is very similar to cytochrome bc 1 (Complex III in mitochondria). Both are transmembrane structures that remove electrons from a mobile, lipid-soluble electron carrier (plastoquinone in chloroplasts; ubiquinone in mitochondria) and transfer them to a mobile, water-soluble electron ...
The main function of PSII is to efficiently split water into oxygen molecules and protons. PSII will provide a steady stream of electrons to PSI, which will boost these in energy and transfer them to NADP + and H + to make NADPH. The hydrogen from this NADPH can then be used in a number of different processes within the plant. [2]
Myosin light chain kinase 4 also known as MYLK4 is an enzyme which in humans is encoded by the MYLK2 gene. [2] MYLK4 is a member of the myosin light-chain kinase family of serine/threonine-specific protein kinases that phosphorylate the regulatory light chain of myosin II .
Thus, myosin phosphatase undoes the muscle contraction process initiated by myosin light-chain kinase. The enzyme is composed of three subunits: the catalytic region (protein phosphatase 1, or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function.
Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. [53] This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments.