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Information on EC 3.5.1.92 - pantetheine hydrolase and Organism(s) Sus scrofa and UniProt Accession Q9BDJ5
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3.5.1.92 pantetheine hydrolaseIUBMB Comments
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant .
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Word Map
- 3.5.1.92
- cysteamine
-
pantothen
-
gpi-anchored
-
ectoenzyme
- pantothenamides
-
gelatinase-associated
-
walter
-
aminothiol
- pantethine
- biotinidase
-
julius
- medicine
- diagnostics
- drug development
The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
vanin-1, pantetheinase, gpi-80, vanin, pagel, vanin 1, pantetheinases, vanin-3, vanin-2, vascular noninflammatory molecule 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(R)-pantetheine amidohydrolase
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5].
CAS REGISTRY NUMBER
COMMENTARY
56093-18-6
-
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
N,N'-bis(pantothenyl)-1,6-diaminohexane + H2O
?
-
96% of the activity with (R)-pantetheine
-
-
?
S-pantetheine 3-pyruvate + H2O
S-cysteamine 3-pyruvate + pantothenate
-
-
S-cysteamine 3-pyruvate spontaneously forms a cyclic product
-
?
pantothenyl-beta-aminoethanol + H2O
?
-
75% of the activity with (R)-pantetheine
-
-
?
NATURAL SUBSTRATE
NATURAL 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Nitro-5-thiocyanobenzoate
-
0.1 mM, 15 min, 10% residual activity in absence of substrate S-pantetheine-3-pyruvate, 51% residual activity in presence of the substrate S-pantetheine-3-pyruvate
5,5'-dithiobis(2-nitrobenzoate)
-
0.1 mM, 15 min, 78% residual activity in absence of substrate S-pantetheine-3-pyruvate, 33% residual activity in presence of the substrate S-pantetheine-3-pyruvate
Bromopyruvate
-
0.1 mM, 15 min, 2% residual activity in absence of substrate S-pantetheine-3-pyruvate, 76% residual activity in presence of the substrate S-pantetheine-3-pyruvate
cystamine
-
0.1 mM, 15 min, 41% residual activity in absence of substrate S-pantetheine-3-pyruvate, 60% residual activity in presence of the substrate S-pantetheine-3-pyruvate
cystine
-
5 mM, 15 min, 100% residual activity in absence of substrate S-pantetheine-3-pyruvate, 32% residual activity in presence of the substrate S-pantetheine-3-pyruvate
H2O2
-
0.1 mM, 15 min, 17% residual activity in absence of substrate S-pantetheine-3-pyruvate, 47% residual activity in presence of the substrate S-pantetheine-3-pyruvate
iodoacetamide
-
0.1 mM, 15 min, 0.5% residual activity in absence of substrate S-pantetheine-3-pyruvate, 72% residual activity in presence of the substrate S-pantetheine-3-pyruvate
iodoacetate
-
1 mM, 15 min, 16% residual activity in absence of substrate S-pantetheine-3-pyruvate, 90% residual activity in presence of the substrate S-pantetheine-3-pyruvate
NaAsO2
-
1 mM, 15 min, 90% residual activity in absence or presence of substrate S-pantetheine-3-pyruvate
NEM
-
1 mM, 15 min, no residual activity in absence of substrate S-pantetheine-3-pyruvate, 54% residual activity in presence of the substrate S-pantetheine-3-pyruvate
o-Iodosobenzoate
-
0.05 mM, 15 min, 15% residual activity in absence of substrate S-pantetheine-3-pyruvate, 53% residual activity in presence of the substrate S-pantetheine-3-pyruvate
p-aminophenylarsine oxide
-
1 mM, 15 min, 45% residual activity in absence of substrate S-pantetheine-3-pyruvate, 55% residual activity in presence of the substrate S-pantetheine-3-pyruvate
PCMB
-
0.0001 mM, 15 min, 1% residual activity in absence of substrate S-pantetheine-3-pyruvate, 68% residual activity in presence of the substrate S-pantetheine-3-pyruvate
Phenylarsine oxide
-
1 mM, 15 min, 48% residual activity in absence of substrate S-pantetheine-3-pyruvate, 52% residual activity in presence of the substrate S-pantetheine-3-pyruvate
additional information
-
no inhibition by 5 mM GSSG in absence or presence of substrate S-pantetheine-3-pyruvate
-
4,4'-dithiodipyridine
-
0.01 mM, 15 min, no residual activity in absence of substrate S-pantetheine-3-pyruvate, 13% residual activity in presence of the substrate S-pantetheine-3-pyruvate
pantethine
-
0.01 mM, 15 min, no residual activity in absence of substrate S-pantetheine-3-pyruvate, 52% residual activity in presence of the substrate S-pantetheine-3-pyruvate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
formation of pantothenic acid allows for a continuous production of CoA, as pantothenic acid is a structural component of this cofactor. In addition, pantothenic acid appears to have profibrotic effects, being involved in the promotion of proliferation and migration of dermal fibroblasts. Moreover, pantothenic acid contributes to restoring CoA levels in the mitochondria, resulting in enhanced mitochondrial activity. Vanin 1 also plays a role in the regulation of a number of metabolic pathways
physiological function
vanin 1 breaks down pantetheine in cysteamine and pantothenic acid, a precursor of coenzyme A. Its physiological role is not strictly related to coenzyme A metabolism, lipid metabolism, and energy production. It also plays a role under physiological conditions in relation to oxidative stress and inflammation. Vanin's enzymatic activity is of key importance in certain diseases, either for its protective effect or as a sensitizer, depending on the diseased organ. But vanin-1's primary function is the recycling of pantothenic acid (vitamin B5), an important precursor in the biosynthesis of coenzymeA (CoA). Vanin 1 also plays a role in the regulation of a number of metabolic pathways
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VNN1_PIG
513
1
57156
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
presence of galactose, mannose, fucose, glucose, galactosamine and sialic acid, 11.8% total carbohydrate content
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after solubilization, the enzsme can be stored indefinitely in the frozen state without significant loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ricci, G.; Nardini, M.; Chiaraluce, R.; Dupre, S.; Cavallini, D.
Interaction of pantetheinase with sulfhydryl reagents and disulfides
Biochim. Biophys. Acta
870
82-91
1986
Sus scrofa
Pitari, G.; Maurizi, G.; Ascenzi, P.; Ricci, G.; Dupre, S.
A kinetic study on pantetheinase inhibition by disulfides
Eur. J. Biochem.
226
81-86
1994
Sus scrofa
Maras, B.; Barra, D.; Dupre, S.; Pitari, G.
Is pantetheinase the actual identity of mouse and human vanin-1 proteins?
FEBS Lett.
461
149-152
1999
Mus musculus, Sus scrofa
Wittwer, C.T.; Burkhard, D.; Ririe, K.; Rasmussen, R.; Brown, J.; Wyse, B.W.; Hansen, R.G.
Purification and properties of a pantetheine-hydrolyzing enzyme from pig kidney
J. Biol. Chem.
258
9733-9738
1983
Sus scrofa
Calvino, J.A.; Barcia, R.
Purification and properties of pantetheinase from pig kidney
J. Food Biochem.
26
103-118
2002
Sus scrofa
Wittwer, C.T.; Wyse, B.W.; Hansen, R.G.
Enzymic hydrolysis of pantetheine
Methods Enzymol.
122
36-43
1986
Sus scrofa
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