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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
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
Topics referred to by the same term
Dipeptidase M may refer to one of two enzymes: X-His dipeptidase Met-X dipeptidase This disambiguation page lists articles associated with the title Dipeptidase
Dipeptidase_M
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
Index of enzymes associated with the same name
Nonspecific dipeptidase may refer to: Membrane dipeptidase, an enzyme Cytosol nonspecific dipeptidase, an enzyme This set index page lists enzyme articles
Nonspecific_dipeptidase
D-Ala-D-Ala dipeptidase (EC 3.4.13.22, D-alanyl-D-alanine dipeptidase, vanX D-Ala-D-Ala dipeptidase, VanX) is an enzyme. This enzyme catalyses the hydrolysis
D-Ala-D-Ala_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
Membrane dipeptidase (EC 3.4.13.19, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase
Membrane_dipeptidase
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
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
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
Xaa-His dipeptidase (EC 3.4.13.3, aminoacylhistidine dipeptidase, carnosinase, homocarnosinase, dipeptidase M) is an enzyme. This enzyme catalyses the
X-His_dipeptidase
Cytosolic non-specific dipeptidase (EC 3.4.13.18) also known as carnosine dipeptidase 2 is an enzyme that in humans is encoded by the CNDP2 gene. This
Cytosol nonspecific dipeptidase
Cytosol_nonspecific_dipeptidase
Dipeptidyl-dipeptidase (EC 3.4.14.6, dipeptidyl tetrapeptide hydrolase, dipeptidyl ligase, tetrapeptide dipeptidase) is an enzyme. This enzyme catalyses
Dipeptidyl-dipeptidase
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
Class of enzymes
Peptidyl-dipeptidase B (EC 3.4.15.4, dipeptidyl carboxyhydrolase, atriopeptin convertase, atrial di-(tri)peptidyl carboxyhydrolase, peptidyldipeptidase
Peptidyl-dipeptidase_B
Met-Xaa dipeptidase (EC 3.4.13.12, methionyl dipeptidase, dipeptidase M) is an enzyme. This enzyme catalyses the following chemical reaction Hydrolysis
Met-X_dipeptidase
Enzyme
Beta-Ala-His dipeptidase (EC 3.4.13.20, serum carnosinase) is an enzyme. This enzyme catalyses the following chemical reaction Preferential hydrolysis
Beta-Ala-His_dipeptidase
Glu-Glu dipeptidase (EC 3.4.13.7, alpha-glutamyl-glutamate dipeptidase, glutamylglutamic arylamidase) is an enzyme. This enzyme catalyses the following
Glu-Glu_dipeptidase
nonspecific dipeptidase and EC 3.4.13.20, β-Ala-His dipeptidase EC 3.4.13.4: Xaa-Arg dipeptidase EC 3.4.13.5: Xaa-methyl-His dipeptidase EC 3.4.13.6:
List_of_EC_numbers_(EC_3)
Xaa-methyl-His dipeptidase (EC 3.4.13.5, anserinase, aminoacyl-methylhistidine dipeptidase, acetylhistidine deacetylase, N-acetylhistidine deacetylase
X-methyl-His_dipeptidase
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
Disease
recessive metabolic disorder caused by a deficiency of carnosinase, a dipeptidase (a type of enzyme that splits dipeptides into their two amino acid constituents)
Carnosinemia
Mammalian protein found in Homo sapiens
Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded
Alanine_aminopeptidase
Chemical compound
created from (S)-lactate and L-phenylalanine by the cytosol nonspecific dipeptidase (CNDP2) protein. It is classified as N-acyl-alpha-amino acid and pseudodipeptide
Lac-Phe
Xaa-Arg dipeptidase (EC 3.4.13.4, aminoacyl-lysine dipeptidase, N2-(4-amino-butyryl)-L-lysine hydrolase, X-Arg dipeptidase) is an enzyme. This enzyme catalyses
X-Arg_dipeptidase
Class of enzymes
Xaa-Pro dipeptidase (EC 3.4.13.9, prolidase, imidodipeptidase, proline dipeptidase, peptidase D, gamma-peptidase) is an enzyme. This enzyme catalyses the
X-Pro_dipeptidase
Non-stereospecific dipeptidase (EC 3.4.13.17, peptidyl-D-amino acid hydrolase, D-(or L-)aminoacyl-dipeptidase) is an enzyme. This enzyme catalyses the
Non-stereospecific dipeptidase
Non-stereospecific_dipeptidase
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
Protein-coding gene in the species Homo sapiens
protein is predicted to enable cysteine-type exopeptidase activity and dipeptidase activity, as well as be involved in proteolysis. It is ubiquitously expressed
SCRN3
Class of enzymes
enzymes include: Various exopeptidases and endopeptidases including dipeptidase and aminopeptidases that convert peptones and polypeptides into amino
Digestive_enzyme
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
Chemical compound
leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and membrane dipeptidase (leukotriene D4 hydrolase). It is being studied for use in the treatment
Ubenimex
Index of enzymes associated with the same name
carboxypeptidase may refer to: Angiotensin-converting enzyme (ACE) Peptidyl-dipeptidase Dcp This set index page lists enzyme articles associated with the same
Dipeptidyl_carboxypeptidase
Protein-coding gene in humans
CM, et al. (2004). "Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells". Protein Expr. Purif. 35 (1): 142–6. doi:10
DPP8
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
Protein-coding gene in the species Homo sapiens
reference expression data Gene ontology Molecular function protein binding dipeptidase activity molecular function Cellular component cytoplasm nuclear membrane
SCRN1
glutathione molecule are removed by gamma-glutamyl transpeptidase and dipeptidases. In the final step, the cystine residue in the conjugate is acetylated
Mercapturic_acid
Set of three coordinated amino acids
acidophilum) PC clan C26, C56 Gamma-glutamyl hydrolase (Rattus norvegicus) S51 Dipeptidase E (Escherichia coli) PD clan C46 Hedgehog protein (Drosophila melanogaster)
Catalytic_triad
Class of enzymes
"Metabolism of leukotrienes by L-gamma-glutamyl-transpeptidase and dipeptidase from human polymorphonuclear granulocytes". Immunology. 55 (1): 135–47
Gamma-glutamyltransferase
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
Chemical compound
synthase, an unidentified gamma-glutamyltransferase, and an unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to
Eoxin_E4
Exopeptidase enzyme that acts on angiotensin I and II
reference expression data Gene ontology Molecular function peptidyl-dipeptidase activity virus receptor activity zinc ion binding endopeptidase activity
Angiotensin-converting enzyme 2
Angiotensin-converting_enzyme_2
Class of enzymes
PB S45, S63 Penicillin G acylase precursor (Escherichia coli) PC S51 Dipeptidase E (Escherichia coli) PE P1 DmpA aminopeptidase (Brucella anthropi) None
Serine_protease
Chemical compound
synthase, an unidentified gamma-glutamyltransferase, and an unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to
Eoxin_A4
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
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
N-formimidoyl derivative of thienamycin, is rapidly metabolized by a renal dipeptidase enzyme found in the human body. To prevent its rapid degradation, imipenem
Thienamycin
Protein-coding gene in the species Homo sapiens
Molecular function peptidase inhibitor activity protein binding peptidyl-dipeptidase inhibitor activity heparan sulfate proteoglycan binding Cellular component
Glypican_3
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
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
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
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
(NC_003063) αr14 gene Atu4112 D 1230719 1231906 NP_356534.2 proline dipeptidase-metalloexopeptidase Agrobacterium tumefaciens str. C58 chromosome linear
Αr14_RNA
Enzyme
activity Ac-Asp-Glu binding hydrolase activity metallopeptidase activity dipeptidase activity Cellular component cytoplasm integral component of membrane
Glutamate_carboxypeptidase_II
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
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
Chemical compound
synthase, an unidentified gamma-glutamyltransferase, and an unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to
Eoxin_C4
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
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
glycosyl-phosphatidylinositol anchors of porcine and human renal membrane dipeptidase. Comprehensive structural studies on the porcine anchor and interspecies
Glypiation
Chemical compound
peptidases and transferases, such as gamma-glutamyl-transpeptidase, dipeptidase, and N-acetyltransferase. The mercapturic acids that can be formed are
Glycidamide
Topics referred to by the same term
Pro X, a Kohavision TV show Cytosol nonspecific dipeptidase, an enzyme also known as Pro-X dipeptidase Lysosomal Pro-X carboxypeptidase, an enzyme Membrane
Pro_X_(disambiguation)
Index of enzymes associated with the same name
Dipeptide hydrolase may refer to: Membrane dipeptidase, an enzyme Angiotensin-converting enzyme, an enzyme This set index page lists enzyme articles associated
Dipeptide_hydrolase
Intestinal enzyme mixture
aminopeptidase, carboxypeptidase and dipeptidase are preferred. The term is now considered obsolete. Erepsin may contain dipeptidases, aminopeptidases, occasionally
Erepsin
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
Protein-coding gene in humans
native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus"
METAP2
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
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
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
Topics referred to by the same term
Peptidase A may refer to: Cytosol nonspecific dipeptidase, an enzyme Penicillopepsin, an enzyme This disambiguation page lists articles associated with
Peptidase_A
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)
Species of bacterium
sanfrancisco CB1: Purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase". Appl Environ Microbiol. 62 (9): 3220–6. Bibcode:1996ApEnM
Limosilactobacillus_pontis
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
Chemical compound
synthase, an unidentified gamma-glutamyltransferase, and an unidentified dipeptidase, respectively, in a pathway which appears similar if not identical to
Eoxin_D4
Family of bacteria
analyses in the proteins dihydrolipoamide succinyltransferase, Xaa-Pro dipeptidase, bifunctional UDP-sugar hydrolase (5'-nucleotidase), transcriptional
Morganellaceae
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)
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 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
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
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
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
Protein structural motif
and Streptomyces mobaraensis), γ-glutamyl transpeptidases, isoaspartyl dipeptidases, and specialised enzymes such as N-acyl homoserine lactone acylases (e
N-terminal nucleophile hydrolases
N-terminal_nucleophile_hydrolases
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