3.4.21.93: Proprotein convertase 1
This is an abbreviated version!
For detailed information about Proprotein convertase 1, go to the full flat file.
Word Map on EC 3.4.21.93
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3.4.21.93
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obesity
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proinsulin
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proglucagon
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subtilisin-like
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endoproteases
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medicine
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tmem18
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proneuropeptides
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drug development
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analysis
- 3.4.21.93
- obesity
- proinsulin
- proglucagon
-
subtilisin-like
- endoproteases
- medicine
-
tmem18
-
proneuropeptides
- drug development
- analysis
Reaction
release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds =
Synonyms
Furin homolog, More, mPC1, mPC1/3, mPC3, mSPC3, murine PC1/3, murine proprotein convertase-1, murine proprotein convertase-1/3, Neuroendocrine convertase 1, PC 1/3, PC1, PC1/3, PC1/PC3, PC3, PCI, PCSK1, prohormone convertase, prohormone convertase 1, prohormone convertase 1/3, Prohormone convertase 3, prohormone convertase PC3, prohormone-convertase 1, propeptide convertase, Propeptide processing protease, proprotein convertase 1, proprotein convertase 1/3, proprotein convertase PC1, proprotein convertase PC1/3, protein convertase 1/3
ECTree
3.4.21.93 Proprotein convertase 1Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.93 - Proprotein convertase 1
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
-
?
cholecystokinin 8-containing peptide + H2O
?
-
a synthetic peptide substrate containing the CCK 8 Gly Arg Arg peptide sequence, i.e. DYMGWMDF, and the cleavage site of pro-cholecystokinin for its liberation, overview
-
-
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
L-pGlu-L-Arg-L-Thr-L-Lys-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pro-cholecystokinin + H2O
N-terminal propeptide + C-terminal cholecystokinin 8 Gly Arg Arg peptide + remaining CCK peptide
-
the substrate is only cleaved in vivo since defolding proteins ar required, in vitro the cleavage site is inaccessible for the enzyme
peptide product analysis
-
?
pro-cholecystokinin + H2O
N-terminal propeptide + cholecystokinin 58
-
the substrate is only cleaved at the CKK 8 peptide in vivo since defolding proteins ar required, in vitro the cleavage site is inaccessible for the enzyme
peptide product analysis
-
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-peptides of islet amyloid polypeptide
-
precursor of IAPP or amylin, the major component of islet amyloid, cleavage at the C- and N-terminus
-
-
?
progastrin + H2O
gastrin-34 + gastrin-17
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PC1/3 initiates cleavage at the N-terminal di-arginine site (Arg36-Arg37) at an early stage in the processing. The endoproteolytic maturation of progastrin in normal G-cells appears to require an interplay, primarily between PC1/3 and PC2. Processing may begin with PC1/3, which is solely responsible for the cleavage of Arg36-Arg37. Subsequently, PC1/3 cleaves the crucial Arg73-Arg74. Later, in secretory granules, PC2 performs the partial cleavage of Lys53-Lys54 to ensure the production of gastrin-17
-
-
?
proglucagon + H2O
glicentin + major proglucagon fragment
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can be differentially processed to produce alternative final products, depending on the cell type in which they are expressed
-
?
proglucagon1-158 + H2O
oxyntomodulin + glicentin-related polypeptide + IP2/GLP-2
-
glicentin lacks the signal sequence of proglucagon, residues -20-1, recombinant hamster substrate and murine enzyme co-expressed in rat GH4C1 cells, low activity, cleavage at the proglucagon interdomain site Lys70-Arg71-/-, and at Lys31-Arg32-/-
mature glucagon consists of residues 33-61, glicentin-related polypeptide comprises the C-terminal residues 1-32, GLP-1 is the N-terminal glucagon-like peptide comprising residues 62-69, IP2/GLP-2 comprises residues 72-158
-
?
proopiomelanocortin + H2O
?
-
is cleaved by prohormone convertase 1/3 to produce peptides that regulate the body's response to energy availability
-
-
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
somatostatin + H2O
?
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PC1 may function as sorting element for somatostatin for its maturation and processing to appropiate targets
-
-
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
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PC1/3 is essential for pro-GIP processing
GIP
-
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
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i.e. pro-GIP, incretin hormone
GIP
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
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posttranslational processing mechanism, PC1 is the primary enzyme involved in the processing, overview
-
-
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
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proGHRH, processing
products are the pro-peptide of 1.7 kDa, the mature GHRH of 5.2 kDa, and GHRH-RP of 3.6 kDa
-
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
-
PC1/3 and furin, EC 3.4.21.75, are major processing enzymes, processing overview
-
-
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
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pro-GHRH, processing, cleavage of C-terminal -RXRXXR-/-, cleavage site specificity determination by substrate mutational analysis, activity with pro-GHRH mutants R8A, R11A, and Q10R, overview
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-
?
Pro-opiomelanocortin + H2O
?
-
the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
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-
?
Pro-opiomelanocortin + H2O
?
-
the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
-
-
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
-
-
-
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
-
small amounts of beta-endorphin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
-
-
-
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
-
small amounts of beta-endorphin
?
pro-thyrotropin-releasing hormone + H2O
fragments of pro-thyrotropin-releasing hormone
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prohormone processing within the regulated secretory pathway of neuroendocrine cells
5 TRH peptide and 7 to 9 other peptides
-
?
pro-thyrotropin-releasing hormone + H2O
fragments of pro-thyrotropin-releasing hormone
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activity with wild-type and mutant pro-TRH, expressed in murine AtT20 cells, recognized epitopes and moieties in pro-TRH by PC1, overview
5 TRH peptide and 7 to 9 other peptides
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?
prodynorphin + H2O
dynorphin + ?
-
hydrolyzes peptide bonds with Tyr at position P2
-
-
?
prodynorphin + H2O
dynorphin + ?
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hydrolyzes peptide bonds with Tyr at position P2
-
-
?
Proinsulin + H2O
?
-
the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
-
-
?
Proinsulin + H2O
?
-
the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
-
-
?
Proinsulin + H2O
Insulin + ?
-
cleaves at both C peptide junctions to release rat insulin I but generates a larger proportion of intermediate cleaved at the B chain-C peptide junction, indicating a preference for this site
-
-
?
Proinsulin + H2O
Insulin + ?
-
cleaves at both C peptide junctions to release rat insulin I but generates a larger proportion of intermediate cleaved at the B chain-C peptide junction, indicating a preference for this site
-
-
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
-
-
-
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
processing and activation of the inactive prohormone is required for regulation of energy balance via leptin, enzyme regulation, overview
-
-
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
processing of the prohormone
-
-
?
additional information
?
-
-
the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
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-
?
additional information
?
-
-
unlike prohormone convertase 2, does not hydrolyze proluteinizing-hormone-releasing-hormone
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-
?
additional information
?
-
-
cleaves precursors both at specific single and pairs of basic residues
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-
?
additional information
?
-
-
biosynthesis of peptide hormones by processing of larger precursors
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?
additional information
?
-
-
key enzyme capable of processing a variety of prohormones to their bioactive forms
-
?
additional information
?
-
-
the enzyme shows specific binding protein 7B2
-
-
?
additional information
?
-
-
a congenital deficiency of prohormone convertase 1/3 which cleaves POMC, AgRP, cholecystokinin, proglucagon, glucagon-like peptide-1 and pro-insulin leads to a syndrome characterized by obesity, small intestinal dysfunction, hyperphagia and dysregulation of glucose homeostasis
-
-
?
additional information
?
-
-
enhanced proprotein convertase 1/3 levels, leading to improved processing of proinsulin and proglucagon, may contribute to the benefits of pioglitazone therapy
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-
?
additional information
?
-
-
unlike prohormone convertase 2, does not hydrolyze proluteinizing-hormone-releasing-hormone
-
-
?
additional information
?
-
-
cleaves precursors both at specific single and pairs of basic residues
-
-
?
additional information
?
-
-
cleaves polypeptide hormones and many proteins at specific sites
-
?
additional information
?
-
-
implicated in processing of proproteins in the secretory pathway, synthesized as a zymogen, cleaves his own profragment in the endoplasmic reticulum
-
?
additional information
?
-
-
the enzyme is involved in the regulated secretory pathway in neuroendocrine cells
-
-
?
additional information
?
-
-
the enzyme is involved in the regulated secretory pathway in neuroendocrine cells, the enzyme activity is regulated by the PC1-propeptide and by proSAAS CT peptide
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-
?
additional information
?
-
-
cleavage site specificity, activity with mutant proglucagon and truncation variants, analysis of importance of substrate domain structure, molecular modeling, overview
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-
?
additional information
?
-
-
PC1/3 CT peptide is not cleaved by enzymatically active PC1/3
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-
?
additional information
?
-
-
prohormone convertase 1/3 mRNA levels in the arcuate nucleus respond normally to signals of energy availability in wild-type mice but not in N2KO mice
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-
?
additional information
?
-
-
key enzyme capable of processing a variety of prohormones to their bioactive forms
-
?
additional information
?
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constitutive secretory pathway
-
?
