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Information on EC 4.1.1.112 - oxaloacetate decarboxylase and Organism(s) Homo sapiens and UniProt Accession Q6P587
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4.1.1.112 oxaloacetate decarboxylaseIUBMB Comments
Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme's involvement in Na+ transport.
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Word Map
- 4.1.1.112
-
klebsiella
- biotin
- carboxybiotin
-
biotin-containing
-
avidin-sepharose
- carboxyltransferase
-
biotin-dependent
- transcarboxylase
-
citps
- modestum
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
oxaloacetate decarboxylase, fahd1, oxalacetate decarboxylase, oxaloacetate decarboxylase na+ pump, oad-2, oad-1, pa4872, fah domain-containing protein 1, oxaloacetate carboxylyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Oxalacetate decarboxylase
-
-
-
-
Oxalacetic acid decarboxylase
-
-
-
-
Oxalacetic beta-decarboxylase
-
-
-
-
Oxalacetic carboxylase
-
-
-
-
Oxalate beta-decarboxylase
-
-
-
-
Oxaloacetate carboxylyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate carboxy-lyase (pyruvate-forming)
Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme's involvement in Na+ transport.
CAS REGISTRY NUMBER
COMMENTARY
9024-98-0
-
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
Oxaloacetate
Pyruvate + CO2
bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
oxaloacetate
-
Y235A mutant, Vmax = 0.2 micromol/min/mg. In the presence of GDP
0.0003
oxaloacetate
-
Y235S mutant, Vmax = 0.1 micromol/min/mg. In the presence of GDP
0.0004
oxaloacetate
-
wild-type, Vmax = 3 micromol/min/mg. In the presence of GDP
0.0004
oxaloacetate
-
Y235F mutant, Vmax = 3 micromol/min/mg. In the presence of GDP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme
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). FAHD1_HUMAN
224
0
24843
Swiss-Prot
Mitochondrion (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
LITERATURE
E33A
H30A
K123A
oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished
additional information
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
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dharmarajan, L.; Case, C.L.; Dunten, P.; Mukhopadhyay, B.
Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate
FEBS J.
275
5810-5819
2008
Homo sapiens
Pircher, H.; von Grafenstein, S.; Diener, T.; Metzger, C.; Albertini, E.; Taferner, A.; Unterluggauer, H.; Kramer, C.; Liedl, K.R.; Jansen-Duerr, P.
Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase
J. Biol. Chem.
290
6755-6762
2015
Homo sapiens (Q6P587)
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
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