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Amino acid
Serine /ˈsɪəriːn/ (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated
Serine
Class of protein kinase enzymes
A serine/threonine protein kinase (EC 2.7.11.-) is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid
Serine/threonine-specific protein kinase
Serine/threonine-specific_protein_kinase
Class of enzymes
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the enzyme's
Serine_protease
Albanian grape variety
Albania. It occurs in two phenotypic forms: "Serinë e Bardhë" (White Serinë) and "Serinë e Zezë" (Black Serinë). Both are used in winemaking, distillation
Serinë
Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. A defining
Serine_hydrolase
InterPro Family
Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular
Serine hydroxymethyltransferase
Serine_hydroxymethyltransferase
Enzyme
Serine dehydratase (SDH), also called L-serine dehydratase/L-threonine deaminase, is an enzyme which in humans is encoded by the gene SDS. SDH is able
Serine_dehydratase
Serine–pyruvate transaminase (EC 2.6.1.51) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction serine + pyruvic acid
Serine–pyruvate_transaminase
Protein-coding gene in the species Homo sapiens
Serine racemase (SR, EC 5.1.1.18) is the first racemase enzyme in human biology to be identified. This enzyme converts L-serine to its enantiomer form
Serine_racemase
Class of enzymes
3-dihydroxybenzoate—serine ligase, EC 6.3.2.14) is an enzyme that catalyzes the chemical reaction ATP + 2,3-dihydroxybenzoate + L-serine ⇌ {\displaystyle
2,3-dihydroxybenzoate—serine ligase
2,3-dihydroxybenzoate—serine_ligase
Class of enzymes
enzymology, a serine C-palmitoyltransferase (EC 2.3.1.50) is an enzyme that catalyzes the chemical reaction: palmitoyl-CoA + L-serine ⇌ {\displaystyle
Serine_C-palmitoyltransferase
Protein domain
Serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L-serine ⇌ {\displaystyle \rightleftharpoons }
Serine_O-acetyltransferase
Unusually stable cluster consisting of eight serine molecules
The Serine octamer cluster in physical chemistry is an unusually stable cluster consisting of eight serine molecules (Ser) implicated in the origin of
Serine_octamer_cluster
Set of three coordinated amino acids
product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine, but occasionally threonine or even selenocysteine. The 3D structure
Catalytic_triad
Enzyme
In enzymology, serine 2-dehydrogenase (EC 1.4.1.7) is an enzyme that catalyzes the chemical reaction serine + NAD+ H2O H+ H2O H+ hydroxypyruvic acid
Serine_2-dehydrogenase
Enzyme found in humans
Serine–tRNA ligase, mitochondrial, also called seryl-tRNA synthetase 2, mitochondrial, is an enzyme that in humans is encoded by the SARS2 gene. Like serine–tRNA
Serine–tRNA ligase, mitochondrial
Serine–tRNA_ligase,_mitochondrial
Protein-coding gene in the species Homo sapiens
Serine protease HTRA1 is an enzyme that in humans is encoded by the HTRA1 gene. The HTRA1 protein is composed of four distinct protein domains. They are
Serine_protease_HTRA1
Class of enzymes
In enzymology, a serine–tRNA ligase (EC 6.1.1.11) is an enzyme that catalyzes the chemical reaction ATP + L-serine + tRNASer ⇌ {\displaystyle \rightleftharpoons
Serine–tRNA_ligase
Chemical compound
is a serine protease inhibitor (serine hydrolase inactivator) commonly used in the preparation of cell lysates. PMSF does not inactivate all serine proteases
PMSF
Class of enzymes
enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase
Carboxypeptidase_D
Class of enzymes
phosphorylated serine/threonine residues: [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate Serine and threonine
Protein serine/threonine phosphatase
Protein_serine/threonine_phosphatase
Kinase enzyme involved in cholesterol homeostasis
[low-density-lipoprotein receptor]-L-serine ⇌ {\displaystyle \rightleftharpoons } ADP + [low-density-lipoprotein receptor]-O-phospho-L-serine Thus, the two substrates
Low-density-lipoprotein receptor kinase
Low-density-lipoprotein_receptor_kinase
Class of enzymes
Serine-phosphoethanolamine synthase (EC 2.7.8.4) is an enzyme that catalyzes the chemical reaction CDP-ethanolamine + L-serine cytidine monophosphate
Serine-phosphoethanolamine synthase
Serine-phosphoethanolamine_synthase
Protein-coding gene in the species Homo sapiens
Serine hydroxymethyltransferase 2 is an enzyme that in humans is encoded by the SHMT2 gene. GRCh38: Ensembl release 89: ENSG00000182199 – Ensembl, May
Serine hydroxymethyltransferase 2
Serine_hydroxymethyltransferase_2
Class of enzymes
Serine-glyoxylate transaminase (EC 2.6.1.45) is a pyridoxal phosphate-dependent enzyme that catalyzes the rversible chemical reaction serine + glyoxylic
Serine—glyoxylate transaminase
Serine—glyoxylate_transaminase
The enzyme Serine-sulfate ammonia-lyase (EC 4.3.1.10) catalyzes the chemical reaction L-serine O-sulfate + H2O ⇌ {\displaystyle \rightleftharpoons } pyruvate
Serine-sulfate_ammonia-lyase
Protein-coding gene in the species Homo sapiens
Serine palmitoyltransferase, long chain base subunit 1, also known as SPTLC1, is a protein which in humans is encoded by the SPTLC1 gene. Serine palmitoyltransferase
SPTLC1
Thermitase (EC 3.4.21.66, thermophilic Streptomyces serine proteinase, Thermoactinomyces vulgaris serine proteinase) is an enzyme. This enzyme catalyses the
Thermitase
In enzymology, serine 3-dehydrogenase (EC 1.1.1.276) is an enzyme that catalyzes the chemical reaction L-serine + NADP+ H+ H+ L-3-oxo-alanine
Serine_3-dehydrogenase
Class of enzymes
Receptor protein serine/threonine kinases (EC 2.7.11.30) are enzyme-linked receptors that belong to protein-serine/threonine kinases. The systematic name
Receptor protein serine/threonine kinase
Receptor_protein_serine/threonine_kinase
Species of bird
The golden greenbul (Calyptocichla serinus) is a member of the bulbul family of passerine birds native to the African tropical rainforest. It is the only
Golden_greenbul
Class of enzymes
(IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each
Tryptophan_synthase
Class of enzymes
CDP-diacylglycerol—serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction CDP-diacylglycerol + L-serine ⇌ {\displaystyle
CDP-diacylglycerol—serine O-phosphatidyltransferase
CDP-diacylglycerol—serine_O-phosphatidyltransferase
Enzyme
The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2 (overall reaction)
Carbamoyl-serine ammonia-lyase
Carbamoyl-serine_ammonia-lyase
Protein found in humans
lectin-associated serine protease-2 (EC 3.4.21.104, MASP-2, MASP2, MBP-associated serine protease-2, mannose-binding lectin-associated serine protease-2, p100
Mannan-binding lectin-associated serine protease-2
Mannan-binding_lectin-associated_serine_protease-2
Psychoactive substance found in plants in the family Apocynaceae
(NRX-1074) B6B21 CCG D-Alanine D-Cycloserine D-Serine DHPG Dimethylglycine Glycine HA-966 L-687,414 L-Alanine L-Serine Milacemide Neboglamine (nebostinel) Rapastinel
Ibogaine
Mammalian protein found in humans
of rapamycin (mTOR), also known as mammalian target of rapamycin, is a serine-threonine protein kinase that regulates cell growth, cell proliferation
MTOR
L-serine-phosphatidylethanolamine phosphatidyltransferase (EC 2.7.8.29, phosphatidylserine synthase 2, serine-exchange enzyme II, PTDSS2 (gene)) is an
L-serine-phosphatidylethanolamine phosphatidyltransferase
L-serine-phosphatidylethanolamine_phosphatidyltransferase
Mannose-binding protein-associated serine protease are serine proteases involved in the complement system. Types include: MASP1 MASP2 mannan-binding lectin
Mannose-binding protein-associated serine protease
Mannose-binding_protein-associated_serine_protease
Enzyme found in humans
Serine–tRNA ligase, cytoplasmic, also called seryl-tRNA synthetase 1 is an enzyme that in humans is encoded by the gene SARS1 (previously SARS). SARS belongs
Serine–tRNA ligase, cytoplasmic
Serine–tRNA_ligase,_cytoplasmic
Process of introducing a phosphate group on to a protein
function of proteins. The amino acids most commonly phosphorylated are serine, threonine, tyrosine, and histidine. These phosphorylations play important
Protein_phosphorylation
Enzyme that adds phosphate groups to other proteins
protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most
Protein_kinase
Clade comprising all crustaceans and hexapods
families (especially those of serine-TCN and AGY): different arthropod lineages are differentially biased in their usage of serine, arginine, and leucine synonymous
Pancrustacea
Protein-coding gene in the species Homo sapiens
subset of neutral serine proteases together with proteoglycans and other immune effector molecules in large cytoplasmic granules. These serine proteases are
GZMM
Enzyme found in humans
Serine protease HTRA2, mitochondrial is an enzyme that in humans is encoded by the HTRA2 gene. This protein is involved in caspase-dependent apoptosis
Serine protease HTRA2, mitochondrial
Serine_protease_HTRA2,_mitochondrial
Chemical compound
attached in ester linkage to the first and second carbon of glycerol and serine attached through a phosphodiester linkage to the third carbon of the glycerol
Phosphatidylserine
Family of digestive enzymes
pieces near the start of the small intestines. More generally, trypsins are serine protease enzymes from the PA clan superfamily, and in humans there are three
Trypsin
Chemical compound
plants. O-Acetylserine is biosynthesized by acetylation of the serine by the enzyme serine transacetylase. The enzyme O-acetylserine (thiol)-lyase, using
O-Acetylserine
Proteolytic enzyme found in Bacillus subtilis
group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at
Subtilisin
Enzyme that cleaves IgA antibodies at certain regions
IgA protease (EC 3.4.21.72, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A protease, immunoglobulin A proteinase)
IgA specific serine endopeptidase
IgA_specific_serine_endopeptidase
Class of enzymes
a Fas-activated serine/threonine kinase (EC 2.7.11.8) is an enzyme that catalyzes the chemical reaction ATP + [Fas-activated serine/threonine protein]
Fas-activated serine/threonine kinase
Fas-activated_serine/threonine_kinase
Protein-coding gene in the species Homo sapiens
Serine protease 57 is a protein that in humans is encoded by the PRSS57 gene. This gene encodes an arginine-specific serine protease and member of the
Serine_protease_57
Protein-coding gene in the species Homo sapiens
Microtubule associated serine/threonine kinase 3 is a protein that in humans is encoded by the MAST3 gene. GRCh38: Ensembl release 89: ENSG00000099308
Microtubule associated serine/threonine kinase 3
Microtubule_associated_serine/threonine_kinase_3
Protein family
mechanisms but can have identity of <10%. The clan contains both cysteine and serine proteases (different nucleophiles). PA clan proteases can be found in plants
PA_clan_of_proteases
Protein found found in humans
Serine/arginine-rich splicing factor 10 is a protein that in humans is encoded by the SRSF10 gene (previously SFRS13A, FUSIP1, or FUSIP2). This gene product
SRSF10
Protein domain
domain is an evolutionary conserved protein domain usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular
Kazal_domain
Bacterial enzyme
D-alanine carboxypeptidase, D-alanyl carboxypeptidase, and serine-type D-Ala-D-Ala carboxypeptidase.) is a bacterial enzyme that catalyzes
DD-Transpeptidase
Pharmaceutical compound
O-butyryl-L-serine or as seryl-butyrate, is an ester conjugate of the short-chain fatty acid butyric acid (butyrate) and the amino acid serine. It is a prodrug
SerBut
Class of enzymes
D-Alanine—D-serine ligase (EC 6.3.2.35, VanC, VanE, VanG) is an enzyme with systematic name D-alanine:D-serine ligase (ADP-forming). This enzyme catalyses
D-alanine—D-serine_ligase
DNA strand exchange
classes of serine recombinases, consisting of the small serine recombinase, the ISXc5 resolvase, the serine transposase, and the large serine recombinase
Site-specific_recombination
Protein-coding gene in the species Homo sapiens
as serine protease inhibitor Kazal-type 5 (SPINK5) is a protein that in humans is encoded by the SPINK5 gene. LEKTI is a large multidomain serine protease
LEKTI
Mammalian protein found in Homo sapiens
ATM serine/threonine kinase or Ataxia-telangiectasia mutated, symbol ATM, is a serine/threonine protein kinase that is recruited and activated by DNA
ATM_serine/threonine_kinase
Protein-coding gene in the species Homo sapiens
ELA2, elastase 2, neutrophil, elaszym, serine elastase, subtype human leukocyte elastase (HLE)) is a serine proteinase in the same family as chymotrypsin
Neutrophil_elastase
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction L-serine = pyruvate + NH3 (overall reaction) (1a) L-serine = 2-aminoprop-2-enoate
L-serine_ammonia-lyase
Chemical data page
to Standard temperature and pressure. Reliability of data general note. ^a 200-274-3 EINECS for Serine ^a CID 617 from PubChem ^a CID 5951 from PubChem
Serine_(data_page)
Class of enzymes
the reversible reaction O-phospho-L(or D)-serine + H2O ⇌ {\displaystyle \rightleftharpoons } L(or D)-serine + phosphate For example, with L-phosphoserine
Phosphoserine_phosphatase
Family of waxy lipid molecules
condensation of palmitate and serine to form 3-keto-dihydrosphingosine. This reaction is catalyzed by the enzyme serine palmitoyl transferase and is the
Ceramide
Set of biochemical processes
concentration of serine in the cell. At high concentrations this enzyme will be inactive and serine will not be produced. At low concentrations of serine the enzyme
Amino_acid_synthesis
Protein-coding gene in the species Homo sapiens
Serine/threonine kinase 17a is a protein that in humans is encoded by the STK17A gene. This gene is a member of the death-associated protein (DAP) kinase-related
STK17A
a-D-galactosaminyl)-L-serine + H2O ⇌ {\displaystyle \rightleftharpoons } D-galactosyl-3-N-acetyl-beta-D-galactosamine + L-serine Thus, the two substrates
Mucinaminylserine mucinaminidase
Mucinaminylserine_mucinaminidase
Rare autosomal recessive human diseases
3-phosphohydroxypyruvate, which is the only way for humans to synthesize serine. This disorder is called Neu–Laxova syndrome in neonates. Homozygous or
D-glycerate dehydrogenase deficiency
D-glycerate_dehydrogenase_deficiency
enzyme serine-ethanolaminephosphate phosphodiesterase (EC 3.1.4.13) catalyzes the reaction L-serine phosphoethanolamine H2O L-serine +
Serine-ethanolaminephosphate phosphodiesterase
Serine-ethanolaminephosphate_phosphodiesterase
Protein-coding gene in the species Homo sapiens
Serine/threonine kinase 11 (STK11) also known as liver kinase B1 (LKB1) or renal carcinoma antigen NY-REN-19 is a protein kinase that in humans is encoded
STK11
Protein-coding gene in humans
Transmembrane protease, serine 2 is an enzyme that in humans is encoded by the TMPRSS2 gene. It belongs to the TMPRSS family of proteins, whose members
TMPRSS2
Chemical compound
Phosphoserine (abbreviated as SEP or J) is an ester of serine and phosphoric acid. Phosphoserine is a component of many proteins as the result of posttranslational
Phosphoserine
Chemical compound
War. DFP irreversibly binds with the enzymes containing serine at the active site, e.g. serine proteases, cholinesterase.[citation needed] The marked toxicity
Diisopropyl_fluorophosphate
Protein-coding gene in the species Homo sapiens
Serine palmitoyltransferase, long chain base subunit 2, also known as SPTLC2, is a protein which in humans is encoded by the SPTLC2 gene. SPTLC2 belongs
SPTLC2
Amino acid
bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples
Threonine
Chemical process of introducing a phosphate
modification in eukaryotes. The most common phospho-amino acid residues are those serine, threonine, and tyrosine at a ratio of 1800:200:1. Phosphorylation of the
Phosphorylation
Process where substrates are converted into more complex products in living organisms
plants, the enzyme serine acetyltransferase catalyzes the transfer of acetyl group from acetyl-CoA onto L-serine to yield O-acetyl-L-serine. The following
Biosynthesis
Broad-spectrum serine protease
alkaline proteinase, Tritirachium album serine proteinase, Tritirachium album proteinase K) is a broad-spectrum serine protease. The enzyme was discovered
Proteinase_K
Streptomyces griseus proteinase A, Streptomyces griseus serine proteinase 3, Streptomyces griseus serine proteinase A) is an enzyme. This enzyme catalyses the
Streptogrisin_A
Amino acid substitutions that mimic a phosphorylated protein
phospho-serine, due to it also carrying a negative charge. Therefore, when an aspartic acid replaces a serine, it is a phosphomimetic of phospho-serine and
Phosphomimetics
Class of enzymes
Tryptase (EC 3.4.21.59) is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast
Tryptase
Molecular process that occurs within living cells
glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational
O-linked_glycosylation
Amino acid
of glycine biosynthesis from serine with serine hydroxymethyl transferase. Serine is then converted to pyruvate by serine dehydratase. In the third pathway
Glycine
pyrazolylalanine synthase (EC 4.2.1.50) catalyzes the chemical reaction L-serine + pyrazole ⇌ {\displaystyle \rightleftharpoons } 3-(pyrazol-1-yl)-L-alanine
Pyrazolylalanine_synthase
Enzyme found in humans
2-diacyl-sn-glycero-3-phospho-L-serine + H2O ⇌ a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+) a 1-acyl-sn-glycero-3-phospho-L-serine + H2O ⇌
Phospholipase_A1_member_A
Set of three serine threonine-specific protein kinases
kinase B (PKB), also known as Akt, is the collective name of a set of three serine/threonine-specific protein kinases: Akt1, Akt2, and Akt3. Akt1 and Akt2
Protein_kinase_B
P38 mitogen-activated protein kinases
A mitogen-activated protein kinase (MAPK or MAP kinase) is a type of serine/threonine-specific protein kinases involved in directing cellular responses
Mitogen-activated protein kinase
Mitogen-activated_protein_kinase
polypeptides with serine or threonine as the C-terminal residue. It is characterized by a single hydrogen bond between the hydroxyl group of the serine or threonine
ST_staple
Protein-coding gene in the species Homo sapiens
Brain-specific serine protease 4 (BSSP-4), also known as serine protease 22 or tryptase epsilon, is an enzyme that in humans is encoded by the PRSS22 gene
PRSS22
Mammalian protein involved in blood clotting
zymogen form of factor XIIa (EC 3.4.21.38), an enzyme of the serine protease (or serine endopeptidase) class. In humans, factor XII is encoded by F12
Factor_XII
leucine-specific serine proteinase, leucine endopeptidase, spinach serine proteinase (leucine specific), spinach leucine-specific serine proteinase, Leu-proteinase)
Leucyl_endopeptidase
Protein-coding gene in the species Homo sapiens
This enzyme's systematic name is (protein)-3-O-(N-acetyl-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase. This enzyme catalyses the removal
Protein_O-GlcNAcase
Enzyme that cleaves other proteins into smaller peptides
mechanisms. Proteases can be classified into seven broad groups: Serine proteases - using a serine alcohol Cysteine proteases - using a cysteine thiol Threonine
Protease
Serine protease
85,000 Mr serine protease that complexes with high-molecular-weight kininogen. PK is the precursor of plasma kallikrein, which is a serine protease that
Prekallikrein
Protein domain
The sedolisin (MEROPS S53) family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members
Sedolisin
IUPAC Nomenclature of a catalyst enzyme
3-O-phospho-L-serine:2-oxoglutarate aminotransferase, SerC, PdxC, 3PHP transaminase) is an enzyme with systematic name O-phospho-L-serine:2-oxoglutarate
Phosphoserine_transaminase
systematic name L-serine hydro-lyase (adding indole, L-tryptophan-forming). This enzyme catalyses the following chemical reaction L-serine + indole ⇌ {\displaystyle
Tryptophan synthase (indole-salvaging)
Tryptophan_synthase_(indole-salvaging)
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