Myosin light-chain phosphatase, more commonly called myosin phosphatase, is an enzyme that dephosphorylates the regulatory light chain of myosin II. Notably, αAK is not only the N-terminal helix of the KD, but also the C-terminal αC helix of CNB-D. The reaction was started by adding cGMP (0–200 μM) and monitored for 1 h by using the rate of NADH absorbance decrease at 340 nm, which is proportional to the rate of ATP hydrolysis.
PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+).
It phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division , and nucleic acid synthesis. Also, the catalytic subunit itself can be down-regulated by phosphorylation. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.
This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). In site 1, the basic AIS in PfPKG is docked against the activation loop of the KD in a manner reported for PKA, with key lysines (K15 and K16) replacing homologous arginines (R94 and R95 in PKAR–RIa) in interacting with the P+1 loop on the KD (SI Appendix, Fig. Furthermore, D361 and P370 take the places of glutamine and arginine, respectively, which are universally conserved in determined cAMP- and cGMP-binding CNBs (35). Natriuretic peptide binding to type I receptors (NPRA and NPRB) on target cells activates their intrinsic GC activity, resulting in a rapid increase in cGMP. To overcome stability issues of PKG in the presence of cGMP, we produced isolated CNBs to capture cGMP-dependent conformational changes in other CNBs. Each PKG subunit contains a catalytic domain and a regulatory domain, and for its activation requires cGMP, which is synthesized by guanylyl cyclases (Reaume & Sokolowski, 2009) (Ch. 4B), such that this regulatory unit is likely the first domain in PfPKG to become occupied as the cellular concentration of cGMP rises.
c-Jun N-terminal kinases (JNKs), were originally identified as kinases that bind and phosphorylate c-Jun on Ser-63 and Ser-73 within its transcriptional activation domain.
When inactive, the PKA holoenzyme exists as a tetramer which consists of two regulatory subunits and two catalytic subunits.
of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.
A UniProt proteome can consist of several components.
The component name refers to the genomic component encoding a set of proteins.
This section provides information on the location and the topology of the mature protein in the cell.
This section provides information on the disease(s) and phenotype(s) associated with a protein.
This subsection of the 'Pathology and Biotech' section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.
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