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  2. Protein kinase - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase

    The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. [1] There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets.

  3. Protein kinase domain - Wikipedia

    en.wikipedia.org/wiki/Protein_kinase_domain

    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 ...

  4. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    Dihydroxyacetone kinase in complex with a non-hydrolyzable ATP analog (AMP-PNP). Coordinates from PDB ID:1UN9. [1]In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates.

  5. Phosphoribulokinase - Wikipedia

    en.wikipedia.org/wiki/Phosphoribulokinase

    Phosphoribulokinase (PRK) (EC 2.7.1.19) is an essential photosynthetic enzyme that catalyzes the ATP-dependent phosphorylation of ribulose 5-phosphate (RuP) into ribulose 1,5-bisphosphate (RuBP), both intermediates in the Calvin Cycle.

  6. Phosphoglycerate kinase - Wikipedia

    en.wikipedia.org/wiki/Phosphoglycerate_kinase

    Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP : 1,3-bisphosphoglycerate + ADP ⇌ glycerate 3-phosphate + ATP. Like all kinases it is a transferase.

  7. GSK-3 - Wikipedia

    en.wikipedia.org/wiki/GSK-3

    Glycogen synthase kinase 3 (GSK-3) is a serine/threonine protein kinase that mediates the addition of phosphate molecules onto serine and threonine amino acid residues. First discovered in 1980 as a regulatory kinase for its namesake, glycogen synthase (GS), [2] GSK-3 has since been identified as a protein kinase for over 100 different proteins in a variety of different pathways.

  8. HIPK2 - Wikipedia

    en.wikipedia.org/wiki/HIPK2

    The protein kinase domain is 330 amino acids long and is located near the N-terminus of the protein. [23] [24] In addition to its kinase domain, HIPK2 has two nuclear localization signals, [25] a SUMO interaction motif, [25] an auto-inhibitory domain [23] a transcriptional co-repression domain, [13] and several interaction domains, including ...

  9. Protein kinase B - Wikipedia

    en.wikipedia.org/wiki/Protein_Kinase_B

    Protein kinase B (PKB), also known as Akt, is the collective name of a set of three serine/threonine-specific protein kinases that play key roles in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration.