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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.
For example, the human genome contains over 40 different myosin genes. These differences in shape also determine the speed at which myosins can move along actin filaments. The hydrolysis of ATP and the subsequent release of the phosphate group causes the "power stroke", in which the "lever arm" or "neck" region of the heavy chain is dragged ...
In enzymology, a myosin-heavy-chain kinase (EC 2.7.11.7) is an enzyme that catalyzes the chemical reaction. ATP + [myosin heavy-chain] ADP + [myosin heavy-chain] phosphate Thus, the two substrates of this enzyme are ATP and myosin heavy-chain, whereas its two products are ADP and myosin heavy-chain phosphate.
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 .
Structurally, myosin light chains belong to the EF-hand family, a large family of Ca 2+ - binding proteins. MLCs contain two Ca 2+ - binding EF-hand motifs. MLCs isoforms modulate the Ca 2+ of force transduction and cross-bridge kinetics. Myosin light chains (MLCs) can be broadly classified into two groups: Essential or alkali MLC (MLC1 or ELC),
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, a structural component of muscle, consists of two heavy chains and four light chains. The protein encoded by this gene is a myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads. The encoded protein binds calcium and is activated by myosin light chain kinase.