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SerineSerine EndopeptidasesSerine ProteasesSerine Proteinase InhibitorsAmino Acid SequencePhosphorylationMolecular Sequence DataSerine C-PalmitoyltransferasePhosphoserineSerine O-AcetyltransferaseGlycine HydroxymethyltransferaseProtein-Serine-Threonine KinasesThreonineSubstrate SpecificityBase SequenceMutagenesis, Site-DirectedSequence Homology, Amino AcidBinding SitesCell LineMutationRecombinant ProteinsKineticsMannose-Binding Protein-Associated Serine ProteasesSerpinsCloning, MolecularEnzyme ActivationProtein BindingProtein KinasesSignal TransductionAmino AcidsL-Serine DehydrataseProtein Structure, TertiaryIsoflurophatePhosphoprotein PhosphatasesProtease InhibitorsPeptide MappingPhenylmethylsulfonyl FluorideTrypsinCathepsin GAmino Acid SubstitutionGlycineEndopeptidasesSequence AlignmentProtein Processing, Post-TranslationalElectrophoresis, Polyacrylamide GelCysteineRacemases and EpimerasesTransfectionPhosphothreonineChymotrypsinPhosphoglycerate DehydrogenaseModels, MolecularPhosphopeptidesAlaninePhosphoproteinsEscherichia coliCells, CulturedStructure-Activity RelationshipPhosphoamino AcidsEnzyme InhibitorsOkadaic AcidProtein Phosphatase 2Catalytic DomainDNA, ComplementaryPeptide FragmentsProtein ConformationRecombinant Fusion ProteinsCasein Kinase IICOS CellsSubtilisinsCatalysisMolecular WeightProtein Kinase CTrypsin InhibitorsBlotting, WesternTyrosineHydrolysisPeptide HydrolasesPancreatic ElastaseSubtilisinLeukocyte ElastaseDNA PrimersKallikreinsPeptidesEnzyme PrecursorsHeLa CellsRNA, Transfer, SerPrecipitin TestsCyclic AMP-Dependent Protein KinasesProteinase Inhibitory Proteins, SecretoryRNA, Messenger14-3-3 ProteinsBacterial ProteinsCarrier ProteinsDNA-Binding ProteinsMembrane ProteinsProto-Oncogene ProteinsEsterasesHydrogen-Ion ConcentrationProto-Oncogene Proteins c-akt
ResiduesProteasesKinasePhosphorylationProteinsProteinCysteineGlycineSynthesisHydrolysisEnzyme that catalyzesMechanismThrombinBiosynthesisHistidineProkaryotesMetabolismPyruvateReactions catalyzedTranscriptionalTranssulfurationChemical reactionsPeptideTissuesCatalysisAmino acidReaction catalyzedBacteriaRegulatesStructureProcessStructuralBiologicalFunctionsActivityProductsConversion
Residues14
  • In addition to autoinhibition, CR3 is also inhibited when the protein is not post-translationally phosphorylated at certain serine and tyrosine residues in the CR2 hinge region. (news-medical.net)
  • STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. (nih.gov)
  • O -linked glycans are most commonly attached to serine or threonine residues through the N -Acetylgalactosamine residue. (neb.com)
  • N-linked glycosylation occurs through the asparagine residues of the protein, while O-linked glycosylation occurs through serine or threonine. (neb.com)
  • Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. (embl.de)
  • OGT transfers O-GlcNAc moieties from UDP-GlcNAc to serine and threonine residues of proteins and O-GlcNAcase (OGA) catalyzes the opposite reaction to remove O-GlcNAc. (nature.com)
  • A group of enzymes that are dependent on cyclic GMP and catalyzes the phosphorylation of serine or threonine residues of proteins. (harvard.edu)
  • Kinases enzymatically catalyse the transfer of a phosphate group from a donor, such as ADP or ATP, to a protein at serine, threonine or tyrosine residues. (ddw-online.com)
  • IRS-1 is phosphorylated on serine, threonine and tyrosine residues in a variety of tissues. (thermofisher.com)
  • The residues of the phosphorylated Serine are referred to as phosphoserine. (vedantu.com)
  • Ubiquitin is normally attached to protein lysine residues, but serine, threonine, cysteine and N-terminal ubiquitination can also occur. (cam.ac.uk)
  • The β-linked N-acetyl-D-glucosamine (GlcNAc) is a post-translational modification of serine and threonine residues catalyzed by the enzyme O-GlcNAc transferase (OGT). (qub.ac.uk)
  • Using site-directed mutagenesis we have shown that both PPDK and PEPS in which the serine and cysteine residues, respectively, were substituted with an alanine the enzymes could be regulated indicating that the serine and cysteine residues, respectively, are not essential for regulation. (scirp.org)
  • Docking data showed that residues Asp94 and His95 were essential for serine acetyltransferase activity of CysE, which were confirmed by site-directed mutagenesis. (bvsalud.org)
Proteases8
  • In biochemistry , serine proteases or serine endopeptidases (newer name) are a class of peptidases ( enzymes that cleave peptide bonds in proteins ) that are characterised by the presence of a serine residue in the active site of the enzyme . (bionity.com)
  • Serine proteases are grouped into clans that share structural homology and then further subgrouped into families that share close sequence homology. (bionity.com)
  • Serine proteases participate in a wide range of functions in the body, including blood clotting , immunity , and inflammation , as well as contributing to digestive enzymes in both prokaryotes and eukaryotes. (bionity.com)
  • The three serine proteases of the chymotrypsin-like clan that have been studied in greatest detail are chymotrypsin , trypsin , and elastase . (bionity.com)
  • Serine proteases catalyze a multi-step covalent catalytic mechanism of peptide bond cleavage. (escholarship.org)
  • It has long been assumed that serine proteases including thrombin carry-out catalysis without significant conformational rearrangement of their stable two-β-barrel structure. (escholarship.org)
  • While the updated catalytic mechanism shares features with the serine proteases, MCP hydrolase-specific chemistry highlights the versatility of the Ser-His-Asp triad. (rcsb.org)
  • The thrombolytic agents available today are serine proteases that work by converting plasminogen to the natural fibrinolytic agent plasmin. (medscape.com)
Kinase7
Phosphorylation1
Proteins6
Protein4
  • Its activation into the serine-protease-like enzyme, activated protein C (aPC), is catalyzed by thrombin when it is bound to the endothelial proteoglycan thrombomodulin. (medscape.com)
  • Like all the amino acid building blocks of protein and peptides, serine can become essential under certain conditions, and is thus important in maintaining health and preventing disease. (hmdb.ca)
  • L-isomer is one and the only form of Serine that is involved in the process of protein synthesis in humans. (vedantu.com)
  • Serine was first obtained in 1865 from the silk protein, which is a specific rich source, by Emil Cramer. (vedantu.com)
Cysteine3
  • A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. (cathdb.info)
  • The amino acid located between the regulatory threonine and the catalytic histidine is highly conserved being serine in PPDK and cysteine in PEPS. (scirp.org)
  • The biosynthesis of cysteine in bacteria is catalyzed by CysE and CysK. (bvsalud.org)
Glycine3
  • Other neurotransmitters, including glycine, D-serine, glutamate, histamine, and γ-aminobutyric acid (GABA), are also synthesized in reactions catalyzed by PLP-dependent enzymes (7) . (oregonstate.edu)
  • In humans, serine is a nonessential amino acid that can be easily derived from glycine. (hmdb.ca)
  • The findings of altered levels of serine and glycine in patients with psychiatric disorders and the severe neurological abnormalities in patients with defects of L-serine synthesis underscore the importance of L-serine in brain development and function. (hmdb.ca)
Synthesis2
  • The first committed step of sphingomyelin synthesis involves the condensation of L-serine and palmitoyl-CoA. (wikipedia.org)
  • L-serine is the predominant source of one-carbon groups for the de novo synthesis of purine nucleotides and deoxythymidine monophosphate. (hmdb.ca)
Hydrolysis4
  • All three enzymes are synthesized by the pancreatic acinar cells, secreted in the small intestine and are responsible for catalyzing the hydrolysis of peptide bonds . (bionity.com)
  • However, BLA efficacy is declining due to resistance mechanisms including the widespread occurrence of β-lactamases, which catalyse β-lactam hydrolysis. (europa.eu)
  • The mechanism whereby chymotrypsin catalyzes the hydrolysis of a peptide bond can be represented in several steps as shown in the figure below. (openmopac.net)
  • Meta-cleavage product (MCP) hydrolases are members of the α/β-hydrolase superfamily that utilize a Ser-His-Asp triad to catalyze the hydrolysis of a C-C bond. (rcsb.org)
Enzyme that catalyzes2
  • Of note, PLP also functions as a coenzyme for glycogen phosphorylase, an enzyme that catalyzes the release of glucose from stored glycogen. (oregonstate.edu)
  • Acetylcholinesterase (AChE) is an enzyme that catalyzes the breakdown of the neurotransmitter acetylcholine that is essential for cognition and memory. (peerj.com)
Mechanism2
  • Subtilisin is evolutionary unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a catalytic triad , to create a nucleophilic serine . (bionity.com)
  • Unlike the serine β-lactamases, the MBLs are structurally and mechanistically unrelated to PBPs, and are not inhibited by current mechanism-based SBL inhibitors. (europa.eu)
Thrombin2
  • Factor Xa is a trypsin-like serine protease that converts the prothrombin zymogen to its active form thrombin and initiates the final stage of the blood coagulation pathway. (inteligand.com)
  • Thrombin catalyzes enzymatic reactions that result in the formation of fibrin, the important binding part for blood clotting. (inteligand.com)
Biosynthesis1
  • The many biochemical reactions catalyzed by PLP-dependent enzymes are involved in essential biological processes, such as hemoglobin and amino acid biosynthesis, as well as fatty acid metabolism . (oregonstate.edu)
Histidine1
Prokaryotes1
Metabolism1
  • In recent years, L-serine and the products of its metabolism have been recognized not only to be essential for cell proliferation, but also to be necessary for specific functions in the central nervous system. (hmdb.ca)
Pyruvate2
  • Pyruvate, orthophosphate dikinase (PPDK) and phosphoenolpyruvate synthetase (PEPS) catalyze the conversion of pyruvate to phosphoenolpyruvate (PEP). (scirp.org)
  • EC 2.7.9.1) catalyzes the reversible conversion of pyruvate to phosphoenolpyruvate (PEP) and is important in C 4 plants as it is generally recognized as catalyzing the rate-limiting step of C 4 photosynthesis [1]. (scirp.org)
Reactions catalyzed1
  • CDDs are slowly metabolized in mammalian tissues via oxidation and reductive dechlorination reactions catalyzed by cytochrome P450 enzymes, followed by conjugation to more polar molecules such as glutathione and glucuronic acid (ATSDR 1998). (cdc.gov)
Transcriptional1
  • Mechanistically, Pyk1-catalyzed H3pT11 directly reduces the binding of Dot1 to chromatin and inhibits Dot1-catalyzed H3K79me3, which leads to transcriptional repression of autophagy genes and reduced autophagy. (nih.gov)
Transsulfuration1
  • In transsulfuration pathway, Hcy is reacted with serine (Ser) to form cystathionine via vitamin B 6 -dependent cystathionine β -synthase (CBS). (hindawi.com)
Chemical reactions1
  • PLP plays a vital role in the function of over 100 enzymes that catalyze essential chemical reactions in the human body (4) . (oregonstate.edu)
Peptide1
  • The serine has an -OH group that is able to act as a nucleophile, attacking the carbonyl carbon of the scissile peptide bond of the substrate. (bionity.com)
Tissues1
  • It is very likely that the predominant source of l-serine will be very different in different tissues and during different stages of human development. (hmdb.ca)
Catalysis1
  • The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all serine protease enzymes. (bionity.com)
Amino acid2
  • Serine (Ser) or L-serine is an alpha-amino acid. (hmdb.ca)
  • It has long been recognized that, in cell cultures, L-serine is a conditional essential amino acid, because it cannot be synthesized in sufficient quantities to meet the cellular demands for its utilization. (hmdb.ca)
Reaction catalyzed1
  • SAH is further hydrolyzed to yield Hcy in a reaction catalyzed by SAH hydrolases. (hindawi.com)
Bacteria1
  • Serine is found in all organisms ranging from bacteria to plants to animals. (hmdb.ca)
Regulates1
  • Here, we report that H3pT11 directly inhibits Dot1-catalyzed H3K79 tri-methylation (H3K79me3) and uncover how this histone crosstalk regulates autophagy and telomere silencing. (nih.gov)
Structure2
  • At the same time, the structure of Serine was established in 1902. (vedantu.com)
  • A 1.6 Å resolution crystal structure of BphD H265Q incubated with HOPDA revealed that the enzyme's catalytic serine was benzoylated. (rcsb.org)
Process1
  • Phosphoprotein phosphatases catalyse the reverse process. (embl.de)
Structural1
  • The methylation of TPSA catalyzed by Rv0560c was subsequently confirmed by LC-MS. Therefore, TPSA as a GlmU acetyltransferase activity inhibitor may offer a structural basis for new anti-tuberculosis drugs. (bvsalud.org)
Biological1
  • Serine acid forms an integral part of the phospholipids class that is found in the biological membrane, where Ethanolamine is an example. (vedantu.com)
Functions1
  • Conserved region 2 (CR2) is a serine-rich region that functions as a hinge on the molecule. (news-medical.net)
Activity1
  • The serine acetyltransferase activity of CysE was detected and its catalytic properties were also determined. (bvsalud.org)
Products1
Conversion2
  • in particular, PLP is the cofactor for the enzyme kynureninase, which catalyzes the conversion of 3-hydroxykynurenine to 3-hydroxyanthranilic acid. (oregonstate.edu)
  • The ability of these substances to catalyze the conversion of plasminogen to plasmin is affected only slightly by the presence or absence of local fibrin clot. (medscape.com)