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Information on EC 3.7.1.5 - acylpyruvate hydrolase
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3.7.1.5 acylpyruvate hydrolaseIUBMB Comments
Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate.
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Word Map
- 3.7.1.5
- gentisate
- maleylpyruvate
- fumarylacetoacetate
- 3-hydroxybenzoate
- naphthalene
- alcaligenes
- salicylate
- fumarate
- putida
-
isomerization
- oxaloacetate
- m-cresol
-
6-hydroxylase
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isofunctional
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fumarylpyruvate hydrolase, acylpyruvate hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylpyruvate hydrolase
FAHD1
fumaroylacetoacetate hydrolase domain-containing protein 1
fumarylpyruvate hydrolase
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3-acylpyruvate + H2O = a carboxylate + pyruvate
acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-C bond
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-acylpyruvate acylhydrolase
Acts on formylpyruvate, 2,4-dioxopentanoate, 2,4-dioxohexanoate and 2,4-dioxoheptanoate.
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CAS REGISTRY NUMBER
COMMENTARY
54004-67-0
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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
acetylpyruvate + H2O
acetate + pyruvate
bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity
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?
additional information
?
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fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, exhibits acylpyruvase activity and hydrolyzes fumarylpyruvate and acetylpyruvate in vitro, several other structural derivatives, e.g. 3-methylacetopyruvate and acetylactone, are not or poorly hydrolyzed
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?
additional information
?
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fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, exhibits acylpyruvase activity and hydrolyzes fumarylpyruvate and acetylpyruvate in vitro, several other structural derivatives, e.g. 3-methylacetopyruvate and acetylactone, are not or poorly hydrolyzed
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?
additional information
?
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fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, exhibits acylpyruvase activity and hydrolyzes fumarylpyruvate and acetylpyruvate in vitro, several other structural derivatives are not or poorly hydrolyzed
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
Mg2+ cannot properly be substituted by Ca2+ or Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.014
pH 7.4, 22°C, purified recombinant wild-type FAHD1, substrate acetylpyruvate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
activity occurs also in strains OH101, MI214, and MI214/1
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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strain M5al grows well on 3-hydroxybenzoate, 2,5-dihydroxybenzoate (gentisate), and 3,4-dihydroxybenzoate (protocatechuate), but does not grow on 4-hydroxybenzoate. Growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumarylpyruvate hydrolase
brenda
additional information
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strain M5al grows well on 3-hydroxybenzoate, 2,5-dihydroxybenzoate (gentisate), and 3,4-dihydroxybenzoate (protocatechuate), but does not grow on 4-hydroxybenzoate. Growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumarylpyruvate hydrolase
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brenda
additional information
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strain M5al grows well on 3-hydroxybenzoate, 2,5-dihydroxybenzoate (gentisate), and 3,4-dihydroxybenzoate (protocatechuate), but does not grow on 4-hydroxybenzoate. Growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumarylpyruvate hydrolase
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brenda
additional information
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ubiquitous expression of FAHD1 in murine tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
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fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, is part of the FAH protein superfamily
evolution
fumaroylacetoacetate hydrolase domain-containing protein 1, FAHD1, is part of the FAH protein superfamily
metabolism
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the enzyme catalyzes the last step in the gentisate pathway for 3-hydroxybenzoate catabolism
metabolism
the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme
metabolism
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the enzyme catalyzes the last step in the gentisate pathway for 3-hydroxybenzoate catabolism
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metabolism
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the enzyme catalyzes the last step in the gentisate pathway for 3-hydroxybenzoate catabolism
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additional information
Asp102 and Arg106 ate important residues for catalysis
Show AA Sequence and Transmembrane Helices (251 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
lentiviral shRNA knockdown of FAHD1 in human umbilical vein cells
additional information
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lentiviral shRNA knockdown of FAHD1 in human umbilical vein cells
additional information
mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities
additional information
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mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities
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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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of FAHD1 in human umbilical vein cells, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of fumarylpyruvate hydrolase
growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of fumarylpyruvate hydrolase
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growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of fumarylpyruvate hydrolase
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growth on 3-hydroxybenzoate and 2,5-dihydroxybenzoate leads to the induction of fumarylpyruvate hydrolase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jones, D.C.N.; Cooper, R.A.
Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
Arch. Microbiol.
154
489-495
1990
Klebsiella pneumoniae, Klebsiella pneumoniae M5al
brenda
Watson, G.K.; Houghton, C.; Cain, R.B.
Microbial metabolism of the pyridine ring. The metabolism of pyridine-3,4-diol (3,4-dihydroxypyridine) by Agrobacterium sp.
Biochem. J.
140
277-292
1974
Agrobacterium sp.
brenda
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
Mus musculus, Homo sapiens (Q6P587), Homo sapiens
brenda
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
brenda
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Release 2023.1 (January 2023)
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