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Dipeptidase E (EC 3.4.13.21, aspartyl dipeptidase, peptidase E, PepE gene product (Salmonella typhimurium)) is an enzyme. This enzyme catalyses the following
Dipeptidase_E
Enzymes secreted by enterocytes into the small intestine
Dipeptidases are enzymes secreted by enterocytes into the small intestine. Dipeptidases hydrolyze bound pairs of amino acids, called dipeptides. Dipeptidases
Dipeptidase
Mammalian protein found in humans
peptidyl dipeptidase I peptidyl-dipeptide hydrolase peptidyldipeptide hydrolase endothelial cell peptidyl dipeptidase peptidyl dipeptidase-4 PDH peptidyl
Angiotensin-converting_enzyme
Set of three coordinated amino acids
Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An
Catalytic_triad
Class of enzymes
specific for the branched polypeptide cyanophycin. It is similar to Dipeptidase E, another S51 family serine protease. The asymmetric unit of cyanophycinase
Cyanophycinase
Membrane dipeptidase (EC 3.4.13.19, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase
Membrane_dipeptidase
Class of enzymes
elastase is employed to determine the exocrine activity of the pancreas, e.g., in cystic fibrosis or chronic pancreatitis. Serum prostate-specific antigen
Serine_protease
Beta-aspartyl-peptidase (EC 3.4.19.5, beta-aspartyl dipeptidase, beta-aspartyl peptidase, beta-aspartyldipeptidase) is an enzyme. This enzyme catalyses
Beta-aspartyl-peptidase
Protein-coding gene in the species Homo sapiens
Dipeptidase 3 (DPEP3) is a protein that in humans is encoded by the DPEP3 gene. This gene encodes a membrane-bound glycoprotein from the family of dipeptidases
Dipeptidase_3
Dipeptidyl-dipeptidase (EC 3.4.14.6, dipeptidyl tetrapeptide hydrolase, dipeptidyl ligase, tetrapeptide dipeptidase) is an enzyme. This enzyme catalyses
Dipeptidyl-dipeptidase
Protein-coding gene in the species Homo sapiens
Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction
Dipeptidase_1
4.13.19: membrane dipeptidase EC 3.4.13.20: β-Ala-His dipeptidase EC 3.4.13.21: dipeptidase E EC 3.4.13.22: D-Ala-D-Ala dipeptidase EC 3.4.13.23:
List_of_EC_numbers_(EC_3)
Protein-coding gene in the species Homo sapiens
Beta-Ala-His dipeptidase is an enzyme that in humans is encoded by the CNDP1 gene. This gene encodes a member of the M20 metalloprotease family. The encoded
CNDP1
Mammalian protein found in Homo sapiens
Dipeptidase 2 (DPEP2) is a protein which in humans is encoded by the DPEP2 gene. DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family
Dipeptidase_2
Chemical compound
property is due to the physicochemical similarities between membrane dipeptidase (MDP), the compound it is usually set to target, and the bacterial
Cilastatin
Class of enzymes
enzymes include: Various exopeptidases and endopeptidases including dipeptidase and aminopeptidases that convert peptones and polypeptides into amino
Digestive_enzyme
Protein-coding gene in humans
dimer interface and substrate specificity of prolyl dipeptidase DPP8". J. Biol. Chem. 281 (50): 38653–62. doi:10.1074/jbc.M603895200. PMID 17040910. v t e
DPP8
Class of enzymes
Peptidyl-dipeptidase Dcp (EC 3.4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is a metalloenzyme found in the cytoplasm of bacterium
Peptidyl-dipeptidase_Dcp
Protein-coding gene in the species Homo sapiens
Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene. Prolidase is an enzyme in humans that plays a crucial
PEPD
Organ in the gastrointestinal tract
brush border enzyme, splits one amino acid at a time. Aminopeptidase and dipeptidase free the end amino acid products. Lipids (fats) are degraded into fatty
Small_intestine
Mammalian protein found in Homo sapiens
1172/JCI114015. PMC 303821. PMID 2564851. Olsen J, Cowell GM, Kønigshøfer E, Danielsen EM, Møller J, Laustsen L, et al. (October 1988). "Complete amino
Alanine_aminopeptidase
Enzyme in humans
and mice. FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity. Several bioactive peptides and structural
Fibroblast activation protein, alpha
Fibroblast_activation_protein,_alpha
glutathione molecule are removed by gamma-glutamyl transpeptidase and dipeptidases. In the final step, the cystine residue in the conjugate is acetylated
Mercapturic_acid
Protein-coding gene in the species Homo sapiens
has been shown to interact with Retinal G protein coupled receptor and Dipeptidase 1. GRCh38: Ensembl release 89: ENSG00000198954 – Ensembl, May 2017 GRCm38:
KIF-binding_protein
Topics referred to by the same term
automation Media Dispatch Protocol, a file transfer protocol Membrane dipeptidase, an enzyme Mini DisplayPort, a digital display interface Management Development
MDP
Chemical compound
leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and membrane dipeptidase (leukotriene D4 hydrolase). It is being studied for use in the treatment
Ubenimex
Protein-coding gene in the species Homo sapiens
aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase". J Immunol. 163 (6): 3092–9. doi:10.4049/jimmunol.163.6.3092. PMID 10477574
DPP7
Chemical compound
Austen KF (1983). "Conversion of leukotriene D4 to leukotriene E4 by a dipeptidase released from the specific granule of human polymorphonuclear leucocytes"
Leukotriene_E4
Class of enzymes
"Metabolism of leukotrienes by L-gamma-glutamyl-transpeptidase and dipeptidase from human polymorphonuclear granulocytes". Immunology. 55 (1): 135–47
Gamma-glutamyltransferase
Biological process of breaking down food
polypeptides that are then broken down by various exopeptidases and dipeptidases into amino acids. The digestive enzymes however are mostly secreted as
Digestion
Family of bacteria
analyses in the proteins dihydrolipoamide succinyltransferase, Xaa-Pro dipeptidase, bifunctional UDP-sugar hydrolase (5'-nucleotidase), transcriptional
Morganellaceae
Chemical compound
unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to the pathway which forms leukotrienes, i.e. LTA4, LTC4,
Eoxin_E4
Chemical compound
unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to the pathway which forms leukotrienes, i.e. LTA4, LTC4,
Eoxin_A4
Class of compounds
residues of LTC4 are removed step-wise by gamma-glutamyltransferase and a dipeptidase to form sequentially LTD4 and LTE4. The decision to form LTB4 versus
Eicosanoid
Breakdown of proteins into smaller polypeptides or amino acids
acids by various enzymes such as carboxypeptidase, aminopeptidase, and dipeptidase. It is necessary to break down proteins into small peptides (tripeptides
Proteolysis
Chemical compound
unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to the pathway which forms leukotrienes, i.e. LTA4, LTC4,
Eoxin_C4
Metabolism of xenobiotics
glutathione molecule are removed by Gamma-glutamyl transpeptidase and dipeptidases. In the final step, the cystine residue in the conjugate is acetylated
Xenobiotic_metabolism
Protein-coding gene in the species Homo sapiens
Adachi H, Tsujimoto M (August 2002). "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis". Journal of Molecular Biology. 321
POLG
N-Acetylated Alpha-Linked Acidic Dipeptidase Like 2 (NAALADL2) is a protein, encoded by the gene NAALADL2 in humans. NAALADL2 shares 25%–26% sequence
NAALADL2
Chemical compound
peptidases and transferases, such as gamma-glutamyl-transpeptidase, dipeptidase, and N-acetyltransferase. The mercapturic acids that can be formed are
Glycidamide
Chemical compound
unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to the pathway which forms leukotrienes, i.e. LTA4, LTC4,
Eoxin_D4
Protein-coding gene in the species Homo sapiens
peptidase C1 family. It exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities. Up to date, eleven human cysteine proteinases have been identified
Cathepsin_Z
Exopeptidase enzyme that acts on angiotensin I and II
1002/path.1570. PMC 7167720. PMID 15141377. Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, et al. (September 2000). "A novel
Angiotensin-converting enzyme 2
Angiotensin-converting_enzyme_2
Mammalian protein found in humans
S2CID 22354304. Chen X (2006). "Biochemical properties of recombinant prolyl dipeptidases DPP-IV and DPP8". Dipeptidyl Aminopeptidases. Advances in Experimental
Dipeptidyl_peptidase-4
Drug discovery and development
that interact covalently with DPP-4 and those that do not. DPP-4 is a dipeptidase that selectively binds substrates that contain proline at the P1-position
Discovery and development of dipeptidyl peptidase-4 inhibitors
Discovery_and_development_of_dipeptidyl_peptidase-4_inhibitors
Polish-American biochemist and historian of science
earliest work there, Fruton tested the stereochemical specificity of dipeptidase. Under the tutelage of fellow Bergmann lab researcher Leonidas Zervas
Joseph_S._Fruton
Class of enzymes
of LTC4 may be removed step-wise by gamma-glutamyltransferase and a dipeptidase to form sequentially LTD4 and LTE4. To varying extents, the other PUFA
Arachidonate_5-lipoxygenase
Species of bacterium
E; Corsetti, A (1996). "The proteolytic system of Lactobacillus sanfrancisco CB1: Purification and characterization of a proteinase, a dipeptidase, and
Limosilactobacillus_pontis
Class of drugs that hinder the action of leukotriene
Arachidonate 5-lipoxygenase inhibitor Antihistamines Hooper NM (2013). Membrane dipeptidase. Handbook of Proteolytic Ezymes. Academic Press. pp. 1670–1673. ISBN 978-0-12-382219-2
Cysteinyl-leukotriene type 1 receptor antagonists
Cysteinyl-leukotriene_type_1_receptor_antagonists
Protein structural motif
G/V acylases (e.g., from E. coli, Bacillus sphaericus, and Streptomyces mobaraensis), γ-glutamyl transpeptidases, isoaspartyl dipeptidases, and specialised
N-terminal nucleophile hydrolases
N-terminal_nucleophile_hydrolases
264.035.570 – 5'-nucleotidase MeSH D23.050.301.264.035.585 – peptidyl-dipeptidase a MeSH D23.050.301.264.035.587 – platelet membrane glycoprotein iib MeSH D23
List_of_MeSH_codes_(D23)
Protein-coding gene in the species Homo sapiens
expression profiles of cDNA microarray". Cancer Sci. 97 (5): 411–9. doi:10.1111/j.1349-7006.2006.00194.x. PMC 11159625. PMID 16630140. S2CID 25739515. v t e
SCRN1
Enzyme
1365-2559.2007.02635.x. PMID 17448023. S2CID 23454712. Yang S, Datta D, Woo E, Duque A, Morozov YM, Arellano J, Slusher BS, Wang M, Arnsten A (Oct 2022)
Glutamate_carboxypeptidase_II
glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. Comprehensive structural studies on the porcine anchor and interspecies
Glypiation
Protein-coding gene in the species Homo sapiens
CO;2-7. PMID 9853964. S2CID 1966827. Huber R, Mazzarella R, Chen CN, Chen E, Ireland M, Lindsay S, et al. (December 1998). "Glypican 3 and glypican 4
Glypican_3
Protein-coding gene in humans
then to LTE4) by cell surface-attached gamma-glutamyltransferase and dipeptidase peptidase enzymes by the sequential removal of the γ-glutamyl and then
Cysteinyl leukotriene receptor 1
Cysteinyl_leukotriene_receptor_1
Chemical compound
metzincins (EC 3.4.15.1). ExPASy: PDOC00129". "EC 3.4.15.1 - Peptidyl-dipeptidase A in contrast to EC 3.4.15.4 atriopeptin. EMBL-EBI: PDOC00129". McArdle
Candoxatril
homologs have been identified in several nitrogen-fixing symbiotic rhizobia (i.e. R. leguminosarum bv.viciae, R. leguminosarum bv. trifolii, R. etli, and several
Αr14_RNA
muramoylpentapeptide carboxypeptidase MeSH D08.811.277.656.350.297 – dipeptidases MeSH D08.811.277.656.350.350 – dipeptidyl peptidases MeSH D08.811.277
List_of_MeSH_codes_(D08)
Protein-coding gene in humans
native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus"
METAP2
Family of proinflammatory eicosanoids
gamma-glutamyltransferase class enzyme EXD4 → EXE4 via unidentified dipeptidase class enzyme The Arachidonic acid + O2 → 15(S)-HpETE → EXA4 → EXC4 →
Eoxin
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E
DIPEPTIDASE E