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Above is a ball-and-stick model of the inorganic phosphate molecule (H PO 4 2−).Colour coding: P (orange); O (red); H (white). The chemical activity of a protein kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group.
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.
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 ...
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.
Structure of Aurora A kinase (PDB: 3E5A) with labeled elements of secondary structure. The catalytic subunits of protein kinases are highly conserved, and the structures of over 280 of the approximately 494 kinase domains from 481 human genes have been determined, [8] leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases. [9]
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 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.
Two-component systems accomplish signal transduction through the phosphorylation of a response regulator (RR) by a histidine kinase (HK). Histidine kinases are typically homodimeric transmembrane proteins containing a histidine phosphotransfer domain and an ATP binding domain, though there are reported examples of histidine kinases in the atypical HWE and HisKA2 families that are not ...