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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Entamoeba histolytica and UniProt Accession Q58P26
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4.1.1.17 ornithine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
-
n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
-
antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
The taxonomic range for the selected organisms is: Entamoeba histolytica
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, odc-paralogue, xodc2, adometdc/odc, ddodc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bODC
-
-
-
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Decarboxylase, ornithine
-
-
-
-
ODC
ODC-paralogue
-
-
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
ODC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
-
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
L-ornithine
putrescine + CO2
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
-
?
L-ornithine
putrescine + CO2
the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview
-
-
?
L-ornithine
putrescine + CO2
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involved in polyamine biosynthesis
-
?
additional information
?
-
no activity using arginine and lysine as substrates
-
-
?
additional information
?
-
-
no activity using arginine and lysine as substrates
-
-
?
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
L-ornithine
putrescine + CO2
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
protein has conserved pyridoxal 5'-phosphate binding residues
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition of the Entamoeba histolytica enzyme by specific irreversible ODC inhibitor alpha-difluoromethylornithine, DFMO, the recombinant enzyme shows altered amino acid sequence and three-dimensional structure, Entamoeba histolytica putative ODC has a putative binding site for DFMO with substituted disrupted amino acids D332, D361, and Y323 by H296, F305, and N334, through which this inhibitor interacts with the protein
-
additional information
-
no inhibition of the Entamoeba histolytica enzyme by specific irreversible ODC inhibitor alpha-difluoromethylornithine, DFMO, the recombinant enzyme shows altered amino acid sequence and three-dimensional structure, Entamoeba histolytica putative ODC has a putative binding site for DFMO with substituted disrupted amino acids D332, D361, and Y323 by H296, F305, and N334, through which this inhibitor interacts with the protein
-
additional information
enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data
-
additional information
-
enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data
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additional information
-
not inhibited by alpha-difluoromethylornithine
-
additional information
-
12-15% inhibition at 4-8 mg/ml by an ethanolic extract from the stem bark of Bursera fagaroides, collected during January 2004 in the region of Capula, Michoacan, Mexico, on ODC activity in vitro and on the growth of Entamoeba histolytica, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.5
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pH 8.0: about 50% of maximal activity, pH 9.5: about 73% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
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
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). Q58P26_ENTHI
413
0
46432
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
48000
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE
90000
gel filtration and SDS-PAGE, protein cross-linked by glutaraldehyde
46000
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminally truncated enzyme, to 2.8 a resolution. Comparison with other ornithine decarboxylase homologs. Resistance to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine, is due to substitution of key substrate binding residues in active site pocket. Additionally, a few more substitutions similar to antizyme inhibitor, a non-functional homologue of ornithine decarboxylases, are present
circular dichroism analysis reveals 39% alpha-helix, 25% beta-sheets and 36% random coils. Modeling of the enzyme dimer shows two separate active sites at the dimer interface with Lys57 and Cys334 residues of opposite monomers contributing to each active site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C334A
mutation of a putative active site at the dimer interface, completely abolishes enzyme activity. Partial restoration of the enzyme activity is observed when inactive K57A and C334A mutants are mixed, confirming that the dimer is the active form
G361Y
mutation at dimer interface, abolishes enzyme activity and destabilizes the dimer
K157A
mutation at dimer interface, abolishes enzyme activity and destabilizes the dimer
K57A
mutation of a putative active site at the dimer interface, completely abolishes enzyme activity. Partial restoration of the enzyme activity is observed when inactive K57A and C334A mutants are mixed, confirming that the dimer is the active form
additional information
additional information
the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview
additional information
-
the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His- and S-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ODC is encoded by a single-copy gene located on a 1900 kb chromosome, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression of the His- and S-tagged enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arteaga-Nieto, P.; Villagomez-Castro, J.C.; Calvo-Mendez, C.; Lopez-Romero, E.
Partial purification and characterization of ornithine decarboxylase from Entamoeba histolytica
Int. J. Parasitol.
26
253-260
1996
Entamoeba histolytica
Arteaga-Nieto, P.; Lopez-Romero, E.; Teran-Figueroa, Y.; Cano-Canchola, C.; Luna Arias, J.P.; Flores-Carreon, A.; Calvo-Mendez, C.
Entamoeba histolytica: purification and characterization of ornithine decarboxylase
Exp. Parasitol.
101
215-222
2002
Entamoeba histolytica
Rosas-Arreguin, P.; Arteaga-Nieto, P.; Reynoso-Orozco, R.; Villagomez-Castro, J.C.; Sabanero-Lopez, M.; Puebla-Perez, A.M.; Calvo-Mendez, C.
Bursera fagaroides, effect of an ethanolic extract on ornithine decarboxylase (ODC) activity in vitro and on the growth of Entamoeba histolytica
Exp. Parasitol.
119
398-402
2008
Entamoeba histolytica, Entamoeba histolytica HM 1:IMSS
Jhingran, A.; Padmanabhan, P.K.; Singh, S.; Anamika, K.; Bakre, A.A.; Bhattacharya, S.; Bhattacharya, A.; Srinivasan, N.; Madhubala, R.
Characterization of the Entamoeba histolytica ornithine decarboxylase-like enzyme
PLoS Negl. Trop. Dis.
2
e115
2008
Entamoeba histolytica (Q58P26), Entamoeba histolytica
Teran-Figueroa, Y.; Arteaga-Nieto, P.; Bethancourt-Rodriguez, A.; Labra-Barrios, M.L.; Luna-Arias, J.P.; Flores-Carreon, A.; Cano-Canchola, C.; Lopez-Romero, E.; Calvo-Mendez, C.
Entamoeba histolytica, heterologous expression and in situ immunolocalization of ornithine decarboxylase (EhODC)
Exp. Parasitol.
123
99-104
2009
Entamoeba histolytica
Preeti, R.J.; Tapas, S.; Kumar, P.; Madhubala, R.; Tomar, S.
Biochemical, mutational and in silico structural evidence for a functional dimeric form of the ornithine decarboxylase from Entamoeba histolytica
PLoS Negl. Trop. Dis.
6
e1559
2012
Entamoeba histolytica (Q58P26), Entamoeba histolytica
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