• enzyme
  • The C-terminal segment of this enzyme constitutes the catalytic domain. (ebi.ac.uk)
  • Protein kinases are also found in bacteria and plants, and include the pseudokinase sub-family, which exhibit unusual features including atypical nucleotide binding and weak, or no, catalytic activity and are part of a much larger pseudoenzyme group of 'degraded' enzyme relatives that are found throughout life, where they take an active participation in mechanistic cellular signaling. (wikipedia.org)
  • This gene encodes a protein with a BIR (baculoviral inhibition of apoptosis protein repeat) domain and a UBCc (ubiquitin-conjugating enzyme E2, catalytic) domain. (wikipedia.org)
  • The domains of the monomer show a fair amount of flexibility suggesting that the enzyme can open in close to bind with the substrate 3-Dehydroshikimate. (wikipedia.org)
  • Disintegrin and metalloproteinase domain-containing protein 33 is an enzyme that in humans is encoded by the ADAM33 gene. (wikipedia.org)
  • fragment
  • Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken. (ebi.ac.uk)
  • Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. (ebi.ac.uk)
  • Since mutation of Leu 817 to Arg abolishes the catalytic activity, Leu 817 is likely located near the active site of guanylate cyclase-A. These results demonstrate that the carboxyl fragment of guanylate cyclase-A is an ideal system for studying the active site of guanylate cyclase-A. (ahajournals.org)
  • substrates
  • Inactive single domain phosphatases can still specifically bind substrates, and protect again dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. (ebi.ac.uk)
  • Broadly speaking, it is composed of three conserved domains characteristic of the Raf kinase family: conserved region 1 (CR1), a Ras-GTP-binding self-regulatory domain, conserved region 2 (CR2), a serine-rich hinge region, and conserved region 3 (CR3), a catalytic protein kinase domain that phosphorylates a consensus sequence on protein substrates. (wikipedia.org)
  • Once B-Raf is activated, a conserved protein kinase catalytic core phosphorylates protein substrates by promoting the nucleophilic attack of the activated substrate serine or threonine hydroxyl oxygen atom on the γ-phosphate group of ATP through bimolecular nucleophilic substitution. (wikipedia.org)
  • The PH domain functions mainly in the interaction of PDPK1 with phosphatidylinositol (3,4)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate which is important in localization and activation of some of membrane associated PDPK1's substrates including AKT. (wikipedia.org)
  • centre
  • The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. (ebi.ac.uk)
  • The polypeptide has a highly conserved modular organisation consisting of an N-terminal DNA-binding domain, a central regulating segment, and a C-terminal or F region accommodating the catalytic centre. (ebi.ac.uk)
  • mechanism
  • Families of aspartic peptidases, and those of unknown catalytic mechanism. (ebi.ac.uk)
  • All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif [ PMID: 9646865 ]. (ebi.ac.uk)
  • homology
  • The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. (ebi.ac.uk)
  • Poly(ADP-ribose) polymerases: homology, structural domains and functions. (ebi.ac.uk)
  • The family members have the highest homology in their kinase domains (53%-98% identical) and differ from most other protein kinases by the presence of the sequence S-I-N instead of A-P-E in kinase domain VIII. (wikipedia.org)
  • B-Raf functional motifs have been determined by analyzing the homology of PKA analyzed by Hanks and Hunter to the B-Raf kinase domain. (wikipedia.org)
  • interactions
  • In its active conformation, B-Raf forms dimers via hydrogen-bonding and electrostatic interactions of its kinase domains. (wikipedia.org)
  • The hemopexin-like domain has been shown to play a functional role in substrate binding and/or in interactions with the tissue inhibitors of metalloproteinases (TIMPs), a family of specific MMP protein inhibitors. (wikipedia.org)
  • Hydrophobic interactions occur between the domains and the NADPH binding site. (wikipedia.org)
  • activity
  • This domain catalyses a demethylase activity with a preference for 3-methylthymidine. (ebi.ac.uk)
  • The role of telomeres and telomerase in cell aging and cancer was established by scientists at biotechnology company Geron with the cloning of the RNA and catalytic components of human telomerase and the development of a polymerase chain reaction (PCR) based assay for telomerase activity called the TRAP assay, which surveys telomerase activity in multiple types of cancer. (wikipedia.org)
  • Motifs IV-VIII play a role in the catalytic activity, while motifs 1-III and X play a role in binding of the cofactor. (wikipedia.org)
  • zinc
  • One of the two zinc ions is present in the active site and is involved in the catalytic processes of the MMPs. (wikipedia.org)
  • The second zinc ion (also known as structural zinc) and the calcium ion are present in the catalytic domain approximately 12 Å away from the catalytic zinc. (wikipedia.org)
  • Little is known about the roles of the second zinc ion and the calcium ion within the catalytic domain, but the MMPs are shown to possess high affinities for structural zinc and calcium ions. (wikipedia.org)
  • contains
  • The head domain folds over the helices and contains a beta tongue group, which may trigger pore formation. (wikipedia.org)
  • Exon 2 contains the junction of the membrane-binding domain and the catalytic domain of b5R, which shows that there are two forms of b5R: a soluble form and a membrane-bound form. (wikipedia.org)
  • cytochrome
  • Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. (wikipedia.org)
  • orientation
  • The activation of PDPK1's main effector, AKT, is believed to require a proper orientation of the kinase and PH domains of PDPK1 and AKT at the membrane. (wikipedia.org)
  • structure
  • The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. (ebi.ac.uk)
  • The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe-Pro-Val-Trp-Phe-Leu-Tyr-Ser-Leu-Leu-Met-Lys. (wikipedia.org)
  • Functional
  • The similarity in the catalytic domains of C5-cytosine methyltransferases and N6 and N4-adenine methyltransferases provided great interest in understanding the basis for functional similarities and dissimilarities. (wikipedia.org)
  • largely
  • The secretion of PCSK9 is largely dependent on the autocleavage of the signal peptide and N-terminal prodomain, though the N-terminal prodomain retains its association with the catalytic domain. (wikipedia.org)
  • fold
  • Nucleosome formation is dependent on the positive charges of the H4 histones and the negative charge on the surface of H2A histone fold domains. (wikipedia.org)