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Serine/threonine protein kinases (EC 2.7.11.1) phosphorylate the OH group of serine or threonine (which have similar side chains). Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP/cGMP, diacylglycerol, and Ca 2+ /calmodulin.
Various other kinases act on small molecules such as lipids, carbohydrates, amino acids, and nucleotides, either for signaling or to prime them for metabolic pathways. Specific kinases are often named after their substrates. Protein kinases often have multiple substrates, and proteins can serve as substrates for more than one specific kinase.
DNA polymerase's ability to slide along the DNA template allows increased processivity. There is a dramatic increase in processivity at the replication fork. This increase is facilitated by the DNA polymerase's association with proteins known as the sliding DNA clamp. The clamps are multiple protein subunits associated in the shape of a ring.
The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases. [2] [3] [4] Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. This functions as an on/off switch for many cellular processes, including metabolism ...
Thus, the two substrates of this enzyme are ATP and 5'-dephospho-DNA, whereas its two products are ADP and 5'-phospho-DNA. Polynucleotide kinase is a T7 bacteriophage (or T4 bacteriophage) enzyme that catalyzes the transfer of a gamma-phosphate from ATP to the free hydroxyl end of the 5' DNA or RNA. The resulting product could be used to end ...
Nucleoside-diphosphate kinases (NDPKs, also NDP kinase, (poly)nucleotide kinases and nucleoside diphosphokinases) are enzymes that catalyze the exchange of terminal phosphate between different nucleoside diphosphates (NDP) and triphosphates (NTP) in a reversible manner to produce nucleotide triphosphates. Many NDP serve as acceptor while NTP ...
In biochemistry, a dual-specificity kinase (EC 2.7.12.1) is a kinase that can act as both tyrosine kinase and serine/threonine kinase.. MEKs, involved in MAP pathways, are principal examples of dual-specificity kinases.
In enzymology, a nucleoside-phosphate kinase (EC 2.7.4.4) is an enzyme that catalyzes the chemical reaction [1]. ATP + nucleoside phosphate ADP + nucleoside diphosphate. Thus, the two substrates of this enzyme are ATP and nucleoside monophosphate, whereas its two products are ADP and nucleoside diphosphate.
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