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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Lactobacillus sp. and UniProt Accession P43099

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.17 ornithine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Lactobacillus sp.
UNIPROT: P43099
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Word Map
The taxonomic range for the selected organisms is: Lactobacillus sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, adometdc/odc, ddodc, odc-paralogue, xodc2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bODC
-
-
-
-
Decarboxylase, ornithine
-
-
-
-
ODC
-
-
-
-
ODC-paralogue
-
-
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-60-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-2,4-Diaminobutyrate
1,3-Diaminopropane + CO2
show the reaction diagram
-
2% of the activity with L-Orn
-
-
?
L-Lys
1,5-diaminopentane + CO2
show the reaction diagram
-
2% of the activity with L-Orn
-
-
?
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminobutyrate
-
-
5-Aminopentanoate
-
-
6-aminohexanoate
-
-
Butylamine
-
-
Hexylamine
-
-
L-2,4-diaminobutyrate
-
-
Lys
-
L-Lys
putrescine
-
-
spermidine
-
-
spermine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
L-Orn
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1040000
-
equilibrium sedimentation
85000
-
12 * 85000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guirard, B.M.; Snell, E.E.
Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a
J. Biol. Chem.
255
5960-5964
1980
Lactobacillus sp.
Manually annotated by BRENDA team
Momany, C.; Ernst, S.; Ghosh, R.; Chang, N.L.; Hackert, M.L.
Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution
J. Mol. Biol.
252
643-655
1995
Lactobacillus sp.
Manually annotated by BRENDA team
Oliveira, M.A.; Carroll, D.; Davidson, L.; Momany, C.; Hackert, M.L.
The GTP effector site of ornithine decarboxylase from Lactobacillus 30a: kinetic and structural characterization
Biochemistry
36
16147-16154
1997
Lactobacillus sp.
Manually annotated by BRENDA team