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Information on EC 3.7.1.5 - acylpyruvate hydrolase and Organism(s) Homo sapiens and UniProt Accession Q6P587

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EC Tree
     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.5 acylpyruvate hydrolase
IUBMB Comments
Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q6P587
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fumarylpyruvate hydrolase, acylpyruvate hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acylpyruvate hydrolase
-
FAH domain-containing protein 1
-
fumaroylacetoacetate hydrolase domain-containing protein 1
-
additional information
cf. EC 3.7.1.2
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-acylpyruvate acylhydrolase
Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
54004-67-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylpyruvate + H2O
acetate + pyruvate
show the reaction diagram
fumarylpyruvate + H2O
fumarate + pyruvate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046 - 0.0819
Acetylpyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.014
pH 7.4, 22°C, purified recombinant wild-type FAHD1, substrate acetylpyruvate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, is part of the FAH protein superfamily
metabolism
the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FAHD1_HUMAN
224
0
24843
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
x * 28000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 18°C, crystal structure of the enzyme (FAHD1) protein in complex with its cofactor Mg2+, cocrystallization with oxalate and high resolution for the enzyme (FAHD1) in complex with oxalate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D102A
site-directed mutagenesis
E33A
significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity
H30A
significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity
K123A
oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished
R106A
site-directed mutagenesis
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant FAHD1 partially from human umbilical vein cells, recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, dioalysis, cation exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in BL21(DE3) Escherichia coli LysS cells
overexpression of FAHD1 in human umbilical vein cells, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pircher, H.; Straganz, G.D.; Ehehalt, D.; Morrow, G.; Tanguay, R.M.; Jansen-Duerr, P.
Identification of human fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) as a novel mitochondrial acylpyruvase
J. Biol. Chem.
286
36500-36508
2011
Homo sapiens (Q6P587), Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Weiss, A.K.H.; Naschberger, A.; Loeffler, J.R.; Gstach, H.; Bowler, M.W.; Holzknecht, M.; Cappuccio, E.; Pittl, A.; Etemad, S.; Dunzendorfer-Matt, T.; Scheffzek, K.; Liedl, K.R.; Jansen-Duerr, P.
Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1
Biochem. J.
475
3561-3576
2018
Homo sapiens (Q6P587), Homo sapiens
Manually annotated by BRENDA team