Results 1 to 10 of about 365,538 (313)
Localization of the Catalytic Domain of Copepod Luciferases: Analysis of Truncated Mutants of the Metridia longa Luciferase [PDF]
Life, 2023 Luciferases from copepods Metridia longa and Gaussia princeps are successfully used as bioluminescent reporters for in vivo and in vitro assays. Here, we report the minimal sequence of copepod luciferases required for bioluminescence activity that was ...
Svetlana V. Markova +3 more
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The Catalytic Domain Mediates Homomultimerization of MT1-MMP and the Prodomain Interferes with MT1-MMP Oligomeric Complex Assembly [PDF]
Biomolecules, 2022 Homomultimerization of MT1-MMP (membrane type 1 matrix metalloproteinase) through the hemopexin, transmembrane, and cytoplasmic domains plays a very important role in the activation of proMMP-2 and the degradation of pericellular collagen.
Marton Fogarasi, Simona Dima
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The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains [PDF]
BMC Genomics, 2007 AbstractBackgroundThe genomes of the three parasitic protozoaTrypanosoma cruzi,Trypanosoma bruceiandLeishmania majorare the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the ...
Brenchley, Rachel +7 more
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Crystal structure of the catalytic domain of human RPTPH. [PDF]
Acta Crystallogr F Struct Biol Commun, 2022 Receptor-type protein tyrosine phosphatases (RPTPs) receive extracellular stimuli and transfer them into cells. They regulate cell growth, differentiation and death via specific signals. They have also been implicated in cancer, diabetes and neurological diseases.
Kim M, Ryu SE.
europepmc +3 more sources
Modulation of catalytic activity in multi-domain protein tyrosine phosphatases. [PDF]
PLoS ONE, 2011 Signaling mechanisms involving protein tyrosine phosphatases govern several cellular and developmental processes. These enzymes are regulated by several mechanisms which include variation in the catalytic turnover rate based on redox stimuli, subcellular
Lalima L Madan +5 more
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Refolding and kinetic characterization of the phosphodiesterase-8A catalytic domain [PDF]
Protein Expression and Purification, 2009 Cyclic nucleotide phosphodiesterase-8 (PDE8) hydrolyzes the second messenger cAMP and is involved in many biological processes such as testosterone production. Although the bacterial and mammalian expression systems have been extensively tried, production of large quantity of soluble and active PDE8 remains to be a major hurdle for pharmacological and ...
Zier, Yan +3 more
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Metabolites, 2022 As an endoplasmic reticulum (ER)-anchored phospholipase, neuropathy target esterase (NTE) catalyzes the deacylation of lysophosphatidylcholine (LPC) and phosphatidylcholine (PC).
Lin He +5 more
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Effects of N-Terminal Non-catalytic Domains on Enzymatic Properties of the Alginate Lyase AlgL7 from Microbulbifer sp. ALW1 [PDF]
Shipin Kexue, 2023 In order to clarify the effect of the non-catalytic carbohydrate-binding module (CBM) and F5/8 type C domains on the enzymatic properties of AlgL7, an alginate lyase from Microbulbifer sp. ALW1, the full-length enzyme AlgL7 and two truncated enzymes: CD1
HUANG Xiaoyi, LI Hebin, CHEN Yanhong, JIANG Zedong, NI Hui, LI Qingbiao, ZHU Yanbing,
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Marine Drugs, 2022 Alginate is abundant in the cell walls of brown algae. Alginate lyases can degrade alginate, and thus play an important role in the marine carbon cycle and industrial production.
Xiao-Meng Sun +7 more
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Importance of the Domain−Domain Interface to the Catalytic Action of the NO Synthase Reductase Domain [PDF]
Biochemistry, 2008 Calmodulin (CaM) activates NO synthase (NOS) by binding to a 20 amino acid interdomain hinge in the presence of Ca (2+), inducing electrons to be transferred from the FAD to the heme of the enzyme via a mobile FMN domain. The activation process is influenced by a number of structural features, including an autoinhibitory loop, the C-terminal tail of ...
Welland, Andrew +4 more
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