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Information on EC 4.1.1.112 - oxaloacetate decarboxylase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HUU1

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.112 oxaloacetate decarboxylase
IUBMB 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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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HUU1
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
oxaloacetate decarboxylase, fahd1, oxalacetate decarboxylase, oad-2, oxaloacetate decarboxylase na+ pump, oad-1, pa4872, fah domain-containing protein 1, oxaloacetate carboxylyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PA4872
member of the PEP mutase/isocitrate lyase superfamily
Oxalacetate decarboxylase
-
-
-
-
Oxalacetic acid decarboxylase
-
-
-
-
Oxalacetic beta-decarboxylase
-
-
-
-
Oxalacetic carboxylase
-
-
-
-
Oxalate beta-decarboxylase
-
-
-
-
Oxaloacetate carboxylyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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 hide
9024-98-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-methyloxaloacetate
2-oxobutanoate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,3-difluoroxaloacetate
-
alpha-ketovalerate
-
Phosphonopyruvate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
3-methyloxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
0.087 - 2.5
oxaloacetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
250
3-methyloxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
7500
oxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
3,3-difluoroxaloacetate
-
1.09
Acetopyruvate
-
6.7
alpha-ketovalerate
-
3
Phosphonopyruvate
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer of dimers, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, aliquots of 10 mg/ml protein in 5 mM MgCl2, 5 mM phosphonopyruvate and 10 mM NaHEPES (pH 7.0) mixed with equal volumes of reservoir solution containing 12% polyethylene glycol 20000 and 0.1 M MES (pH 6.0)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H235A
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
H235Q
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Y212F
25fold reduction of the Km value compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, phenyl-Sepharose columnn chromatography, and butyl-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Narayanan, B.C.; Niu, W.; Han, Y.; Zou, J.; Mariano, P.S.; Dunaway-Mariano, D.; Herzberg, O.
Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily
Biochemistry
47
167-182
2008
Pseudomonas aeruginosa (Q9HUU1), Pseudomonas aeruginosa
Manually annotated by BRENDA team