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Enzyme found in humans
Carboxypeptidase E (CPE), also known as carboxypeptidase H (CPH) and enkephalin convertase, is an enzyme that in humans is encoded by the CPE gene. This
Carboxypeptidase_E
Class of enzymes
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of
Carboxypeptidase
Protein family
Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains
Carboxypeptidase_A
Class of enzymes
Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes
Carboxypeptidase_D
Peptide hormone that plays a role in glycemic regulation
molecule by proprotein convertase 1/3 (PC1/3). At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. The terminal
Amylin
Hormones and neuropeptides
the trans-Golgi network, POMC binds to a membrane-bound protein, carboxypeptidase E (CPE). CPE facilitates POMC transport into immature budding vesicles
Endorphins
Index of enzymes associated with the same name
hydrolase may refer to the following enzymes: Lysine carboxypeptidase Carboxypeptidase E This set index page lists enzyme articles associated with
Peptidyl-L-lysine(-L-arginine) hydrolase
Peptidyl-L-lysine(-L-arginine)_hydrolase
Topics referred to by the same term
Carbapenemase-producing enterobacteriaceae, a "superbug" resistant to antibiotics Carboxypeptidase E, an enzyme involved in the biosynthesis of neuropeptides and peptide
CPE
Protein family
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). Members of the
Zinc_carboxypeptidase
Protein-coding gene in the species Homo sapiens
lysosomal gamma-glutamyl carboxypeptidase, gamma-Glu-X carboxypeptidase, pteroyl-poly-gamma-glutamate hydrolase, carboxypeptidase G, folic acid conjugase
Gamma-glutamyl_hydrolase
Mouse used for scientific research
to simulate a human disease Obese mice, prone to obesity due to a carboxypeptidase E deficiency Strong muscular mice, with a disabled myostatin gene, nicknamed
Laboratory_mouse
Peptide hormone
the middle part of the protein, called the "C-peptide". Finally, carboxypeptidase E removes two pairs of amino acids from the protein's ends, resulting
Insulin
Mammalian protein found in Homo sapiens
include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase
Proopiomelanocortin
Protein found in humans
endoplasmic reticulum and secreted from dense-core vesicles. It binds carboxypeptidase E (CPE), and disruption of this binding has been proposed to cause the
Brain-derived neurotrophic factor
Brain-derived_neurotrophic_factor
Hu X, Li H, Lin Y, Townsend RR, Polonsky KS, Johnson JD (2008). "Carboxypeptidase E mediates palmitate-induced beta-cell ER stress and apoptosis". Proceedings
Endoplasmic reticulum stress in beta cells
Endoplasmic_reticulum_stress_in_beta_cells
Enzyme
cancer or oncology, PSMA. All refer to the same protein glutamate carboxypeptidase II. GCPII is expressed in many tissues of the body, including prostate
Glutamate_carboxypeptidase_II
Chemical compound
then, the resulting intermediates are further reduced by the enzyme carboxypeptidase E (CPE; previously known as enkephalin convertase (EC)). Proenkephalin
Met-enkephalin
Class of enzymes
lysine and/or arginine residues; these are subsequently removed by carboxypeptidase E. Current scientific evidence indicates that both up- and down-regulation
Proprotein_convertase
Alanine carboxypeptidase (EC 3.4.17.6, N-benzoyl-L-alanine-amidohydrolase) is an enzyme. This enzyme catalyses the following chemical reaction Release
Alanine_carboxypeptidase
Protein-coding gene in the species Homo sapiens
C-terminal basic residues is required; this step is mediated by carboxypeptidases E and/or D. PC2 plays only a minor role in the first step of insulin
Proprotein_convertase_2
Bacterial enzyme
DD-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanine carboxypeptidase, D-alanyl carboxypeptidase,
DD-Transpeptidase
Enzyme
Metallocarboxypeptidase D (EC 3.4.17.22, carboxypeptidase D (cattle, human, mouse, rat), gp180 (duck)) is an enzyme. This enzyme catalyses the following
Metallocarboxypeptidase_D
Potato carboxypeptidase inhibitor (PCI) is a naturally occurring protease inhibitor peptide in potatoes that can form complexes with several metallo-carboxypeptidases
Potato carboxypeptidase inhibitor
Potato_carboxypeptidase_inhibitor
Muramoyltetrapeptide carboxypeptidase (EC 3.4.17.13, carboxypeptidase IIW, carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase)
Muramoyltetrapeptide carboxypeptidase
Muramoyltetrapeptide_carboxypeptidase
Opioid peptide
protease cathepsin L. Under normal circumstances, in the presence of carboxypeptidase E, prodynorphin is fully processed by sequential cleavage at dibasic
Big_dynorphin
Obesity caused by a mutation in a single gene
progonadotropin, require cleavage at the C-terminal basic residues. Carboxypeptidase E (Cp3) is responsible for the prohormone/propeptide cleavage at the
Monogenic_obesity
Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, deamidase, lysosomal carboxypeptidase
Carboxypeptidase_C
Enzyme encoded in humans by the gene CPB2
Carboxypeptidase B2 (CPB2), also known as carboxypeptidase U (CPU), plasma carboxypeptidase B (pCPB) or thrombin-activatable fibrinolysis inhibitor (TAFI)
Carboxypeptidase_B2
17.4, Gly-Xaa carboxypeptidase EC 3.4.17.10: carboxypeptidase E EC 3.4.17.11: glutamate carboxypeptidase EC 3.4.17.12: carboxypeptidase M EC 3.4.17.13:
List_of_EC_numbers_(EC_3)
Carboxypeptidase M (EC 3.4.17.12) is an enzyme that in humans is encoded by the CPM gene. Carboxypeptidase M is a membrane-bound arginine/lysine carboxypeptidase
Carboxypeptidase_M
Protein-coding gene in humans
similarities: the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory
CPD_(gene)
Class of enzymes
examples of exopeptidases include: Carboxypeptidase A - cleaves C-terminal Phe, Tyr, Trp, or Leu Carboxypeptidase B - cleaves C-terminal Lys or Arg Aminopeptidase
Exopeptidase
Protein family
In molecular biology, the carboxypeptidase A inhibitor family is a family of proteins which is represented by the well-characterised metallocarboxypeptidase
Carboxypeptidase_A_inhibitor
Gly-Xaa carboxypeptidase (EC 3.4.17.4, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast carboxypeptidase) is an
Gly-X_carboxypeptidase
Protein-coding gene in the species Homo sapiens
Carboxypeptidase X, M14 family member 2 is a protein that in humans is encoded by the CPXM2 gene. GRCh38: Ensembl release 89: ENSG00000121898 – Ensembl
Carboxypeptidase X, M14 family member 2
Carboxypeptidase_X,_M14_family_member_2
Protein-coding gene in humans
Carboxypeptidase A4 is an enzyme that in humans is encoded by the CPA4 gene. This gene is a member of the carboxypeptidase A/B subfamily, and it is located
CPA4_(gene)
Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme. This enzyme catalyses the following chemical reaction Release of a C-terminal amino acid with broad specificity
Carboxypeptidase_Taq
Enzyme found in humans
Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 gene. The "CPA3" gene expression
CPA3
Chemical compound
been found to affect the activity of carboxypeptidase H and phenylmethylsulfonylfluoride-inhibited carboxypeptidase in rat nervous system tissue. Selank
Selank
Protein-coding gene in the species Homo sapiens
Carboxypeptidase A1 is an enzyme that in humans is encoded by the CPA1 gene. Three different forms of human pancreatic procarboxypeptidase A have been
Carboxypeptidase_A1
Protein-coding gene in humans
Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene. The "CPVL" gene is expressed mainly in monocytes and macrophages
CPVL
Protein-coding gene in the species Homo sapiens
is encoded by the AEBP1 gene. AE binding protein 1 is a member of carboxypeptidase A protein family. The protein may function as a transcriptional repressor
AE_binding_protein_1
Protein-coding gene in the species Homo sapiens
Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. Three different forms of human pancreatic procarboxypeptidase A have been
Carboxypeptidase_A2
Class of enzymes
4.15.5, dipeptidyl carboxypeptidase (Dcp), dipeptidyl carboxypeptidase) is a metalloenzyme found in the cytoplasm of bacterium E. Coli responsible for
Peptidyl-dipeptidase_Dcp
Glutamate carboxypeptidase (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate
Glutamate_carboxypeptidase
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
protein-specific sequence differences.[citation needed] 1968 – Papain 1969 – Carboxypeptidase A is a zinc metalloprotease. Its crystal structure (PDB file 1CPA)
List of biophysically important macromolecular crystal structures
List_of_biophysically_important_macromolecular_crystal_structures
Mammalian protein found in humans
epithelial cells. ACE is also known by the following names: dipeptidyl carboxypeptidase I peptidase P dipeptide hydrolase peptidyl dipeptidase angiotensin
Angiotensin-converting_enzyme
American chemist (1919–2011)
for each turn of a helix. Carboxypeptidase A (left) was the first protein structure from Lipscomb's group. Carboxypeptidase A is a digestive enzyme, a
William_Lipscomb
Protein-coding gene in humans
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene. Carboxypeptidase N is a plasma metallo-protease that cleaves
CPN1
Protein-coding gene in humans
Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene. This gene encodes a member of the metallocarboxypeptidase family. This enzyme
CPZ_(gene)
Enzyme
Retinoid-inducible serine carboxypeptidase is an enzyme that in humans is encoded by the SCPEP1 gene. Carboxypeptidase Serine carboxypeptidase Retinoid GRCh38:
SCPEP1
procollagen C-terminal peptidase, procollagen C-proteinase, procollagen carboxypeptidase, procollagen carboxy-terminal proteinase, procollagen peptidase) is
Procollagen_C-endopeptidase
Liquid secreted by the pancreas
digestive enzymes, including trypsinogen, chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases, and amylase. The pancreas is located
Pancreatic_juice
Protein-coding gene in the species Homo sapiens
other human cysteine proteases. It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin
Cathepsin_Z
Chemical element with atomic number 30 (Zn)
blood, was shown to have zinc in its active site. The digestive enzyme carboxypeptidase became the second known zinc-containing enzyme in 1955. Zinc is the
Zinc
Group of antibiotics derived from fungi
acylates the active site of Bacillus stearothermophilus D-alanine carboxypeptidase". The Journal of Biological Chemistry. 255 (9): 3977–3986. doi:10
Penicillin
Protein-coding gene in the species Homo sapiens
PMID 12975309. Ghose S, Weickert CS, Colvin SM, et al. (2004). "Glutamate carboxypeptidase II gene expression in the human frontal and temporal lobe in schizophrenia"
CNDP1
Medical condition
pancreas secreting active enzymes such as trypsin, chymotrypsin and carboxypeptidase, instead of their inactive forms, leading to auto-digestion of the
Acute_pancreatitis
Protein-coding gene in the species Homo sapiens
Carboxypeptidase A6 (CPA6) is a metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene. It is highly expressed in the adult mouse olfactory
Carboxypeptidase_A6
N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) Leucyl/cystinyl aminopeptidase (LNPEP) Angiotensin-converting
Enkephalinase
Protein-coding gene in humans
Carboxypeptidase N subunit 2 is an enzyme that in humans is encoded by the CPN2 gene. GRCh38: Ensembl release 89: ENSG00000178772 – Ensembl, May 2017 GRCm38:
CPN2
Genus of roundworms
Ascaris species inhibit MCPs by releasing an enzyme known as Ascaris carboxypeptidase inhibitor (ACI). This enzyme binds to the active site of MCP and blocks
Ascaris
Exopeptidase enzyme that acts on angiotensin I and II
F, Baronas E, Godbout K, Gosselin M, Stagliano N, et al. (September 2000). "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts
Angiotensin-converting enzyme 2
Angiotensin-converting_enzyme_2
Foodstuffs obtained by protein hydrolysis
is "Protana Prime", a mixture with both leucine aminopeptidase and carboxypeptidase D activity. Beyond proteolysis, the amount of umami taste can also
Hydrolyzed_vegetable_protein
Immune cell found in connective tissue
tissue mast cells contain heparin and large amounts of histamine and carboxypeptidase in their granules, and are distributed in the skin, peritoneal cavity
Mast_cell
Human viral infection
that the receptor in the closely related duck hepatitis B virus is carboxypeptidase D. The virions bind to the host cell via the preS domain of the viral
Hepatitis_B
Type of α-amino acid
blockage by D-phenylalanine of enkephalin degradation by the enzyme carboxypeptidase A. Enkephalins act as agonists of the mu and delta opioid receptors
Phenylalanine
Protein-coding gene in humans
Probable carboxypeptidase X1 is an enzyme that in humans is encoded by the CPXM1 gene. The protein encoded by this gene is a member of the M14 family of
CPXM1
Organ in the gastrointestinal tract
secreted by the pancreas and cleave proteins into smaller peptides. Carboxypeptidase, which is a pancreatic brush border enzyme, splits one amino acid at
Small_intestine
Cleavage of chemical bonds by the addition of water
Those fragments are then broken down into single amino acids via carboxypeptidases secreted by the pancreas. However, proteases do not catalyze the hydrolysis
Hydrolysis
Species of fungus
encoding secreted proteins, including subtilisins, chitinases, and carboxypeptidases, which assist in degrading nematode eggshells. Pochonia chlamydosporia
Pochonia_chlamydosporia
Hormone
the C-terminal side of the flanking Lys-Arg or Arg-Arg. Second, a carboxypeptidase removes the Lys/Arg residues leaving Gly as the C-terminal residue
Thyrotropin-releasing_hormone
Protein-coding gene in humans
Carboxypeptidase A5 is an enzyme that in humans is encoded by the CPA5 gene. Carboxypeptidases have functions ranging from digestion of food to selective
CPA5
Enzyme
exopeptidases which remove individual amino acids at both ends of proteins (carboxypeptidases produced by the pancreas and aminopeptidases secreted by the small
Pepsin
Enzyme known as Human Protective Protein
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene. The enzyme is also known
Cathepsin_A
Protein family
11-residue and a 41-residue chain. The Carboxypeptidase inhibitor I68 family represents a family of carboxypeptidase inhibitors found in ticks. The peptidase
Protease_inhibitor_(biology)
Breakdown of proteins into smaller polypeptides or amino acids
chymotrypsin, and elastase, and into amino acids by various enzymes such as carboxypeptidase, aminopeptidase, and dipeptidase. It is necessary to break down proteins
Proteolysis
Class of enzymes
aromatic amino acids. Chymotrypsinogen can also be activated by trypsin. Carboxypeptidase, which is a protease that takes off the terminal amino acid group from
Digestive_enzyme
Enzyme that cleaves other proteins into smaller peptides
acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A); others attack internal peptide bonds of a protein (endopeptidases
Protease
Type of enzyme
"metallo carboxypeptidase", "metallo-carboxypeptidase" and "metallocarboxypeptidase" are used to describe a metalloexopeptidase carboxypeptidase. These
Metalloexopeptidase
Part of the immune system that enhances the ability of antibodies and phagocytic cells
this is not universally accepted ) and is usually rapidly cleaved by carboxypeptidase B. Both C3a and C5a have anaphylatoxin activity, directly triggering
Complement_system
Filamentous fungus
Enzymes: strong secretion of amylases (α-amylase and glucoamylase); some carboxypeptidase; low tyrosinase Aesthetics: pleasant fragrance; accumulation of flavoring
Aspergillus_oryzae
Species of bacterium
T; Aoyagi, T (August 1996). "Piperastatin B: a new selective serine carboxypeptidase inhibitor from Streptomyces lavendofoliae MJ908-WF13". Journal of Enzyme
Streptomyces_lavendofoliae
Topics referred to by the same term
Photochemical internalization, a light-triggered drug delivery method Potato carboxypeptidase inhibitor, a natural peptide usable for thrombolytic and cancer therapy
PCI
Chemical compound
carboxy-terminal is now susceptible to the action of the second enzyme, carboxypeptidase β. The leukokinin-S so nicked is present in tissues and blood, free
Tuftsin
Field of chemistry
applications to diagnosis and therapies. Examples: hemoglobin, methylmercury, carboxypeptidase This important area focuses on structure, bonding, and the physical
Inorganic_chemistry
Compound with a metal center bound to ligands
hemoglobin, the cytochromes, the chlorin group in chlorophyll, and carboxypeptidase, a hydrolytic enzyme important in digestion. Another complex ion enzyme
Coordination_complex
Medical condition
"Germinoma" at Dorland's Medical Dictionary Germinoma, Central Nervous System at eMedicine "Pathology". Retrieved 2007-11-03. Germinoma at the U.S. National
Germinoma
Drug discovery
acid) was described to be the most potent inhibitor of carboxypeptidase A in the early 1980s. The authors referred to it as a by-product analog
Discovery and development of ACE inhibitors
Discovery_and_development_of_ACE_inhibitors
Protein-coding gene in the species Homo sapiens
"Comparison of the enzymatic and functional properties of three cytosolic carboxypeptidase family members". The Journal of Biological Chemistry. 290 (2): 1222–32
AGBL4
Class of medications used primarily to treat high blood pressure
colleagues used peptide analogs to study the structure of ACE, using carboxypeptidase A as a model. Their discoveries led to the development of captopril
ACE_inhibitor
APP), and sortilin. Early study on sorting of acid hydrolases such as carboxypeptidase Y (CPY) in S. cerevisiae mutants has led to the identification of retromer
Retromer
Protein-coding gene in the species Homo sapiens
responsive element binding gene downstream and mRNA carboxypeptidase and serine carboxypeptidase gene upstream GRCh38: Ensembl release 89: ENSG00000255690
TLR4 interactor with leucine rich repeats
TLR4_interactor_with_leucine_rich_repeats
Chemical compound
II), neprilysin, NEP2, aminopeptidase P (APP), carboxypeptidase N (CPN, kininase I), Carboxypeptidase M, Neutral endopeptidase 24.15, Endothelin converting
Bradykinin
Polymer of tubulin that forms part of the cytoskeleton
modification are often referred to as Glu-microtubules. Although the tubulin carboxypeptidase has yet to be identified, the tubulin—tyrosine ligase (TTL) is known
Microtubule
Protein-coding gene in the species Homo sapiens
Lysosomal Pro-X carboxypeptidase is an enzyme that in humans is encoded by the PRCP gene. The protein encoded by this gene is a lysosomal prolylcarboxypeptidase
PRCP
Pharmaceutical compound
following radical prostatectomy". Cancer Biotherapy & Radiopharmaceuticals. 14 (2): 99–111. doi:10.1089/cbr.1999.14.99. PMID 10850293. v t e v t e v t e
Indium (111In) capromab pendetide
Indium_(111In)_capromab_pendetide
Hydrolytic enzyme encoded on human chromosome 17
hydrolases such as carboxypeptidaseA. However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the active site
Aspartoacylase
Chemical compound
peptidases. Peptidases such as the serine peptidases, carboxypeptidase N and carboxypeptidase M cleave kinins into des-Arg-bradykinin and Lys-des-Arg-bradykinin
Kallidin
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E
CARBOXYPEPTIDASE E