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Information on EC 4.1.1.74 - indolepyruvate decarboxylase and Organism(s) Enterobacter cloacae and UniProt Accession P23234
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EC Tree
4.1.1.74 indolepyruvate decarboxylaseIUBMB Comments
Thiamine diphosphate- and Mg2+-dependent. More specific than EC 4.1.1.1 pyruvate decarboxylase
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Word Map
- 4.1.1.74
- iaa
- azospirillum
- cloacae
- enterobacter
- brasilense
-
growth-promoting
- decarboxylases
- indole-3-acetaldehyde
- l-tryptophan
-
zymomonas
- tryptophol
- mobilis
-
2-keto
- benzoylformate
- phenylpyruvate
-
diphosphate-dependent
- synthesis
The taxonomic range for the selected organisms is: Enterobacter cloacae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
indolepyruvate decarboxylase, indole-3-pyruvate decarboxylase, indole-3-pyruvic acid decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, indolepyruvate
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-
-
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Decarboxylase, indolepyruvate (Enterobacter agglomerans clone pMB2 gene ipdC reduced)
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-
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GenBank L80006-derived protein GI 1507711
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-
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Indole-3-pyruvate decarboxylase
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Indolepyruvate decarboxylase
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-
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Indolepyruvate decarboxylase (Enterobacter herbocola strain 299R clone pMB2 gene ipdC reduced)
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Indolepyruvic acid decarboxylase
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-
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IpdC
IpdC
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2
residues E468, D29, and H115 are involved in binding of all substrates and decarboxlation of the respective tetrahedral thiamine-diphosphate-substrate adducts. Residue E383 is central to substrate specificity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
3-(indol-3-yl)pyruvate carboxy-lyase [(2-indol-3-yl)acetaldehyde-forming]
Thiamine diphosphate- and Mg2+-dependent. More specific than EC 4.1.1.1 pyruvate decarboxylase
CAS REGISTRY NUMBER
COMMENTARY
183213-32-3
-
9074-92-4
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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
pyruvic acid
acetaldehyde + CO2
-
decarboxylation at 19% of the indole-3-acetic acid decarboxylation
-
-
?
3-(indol-3-yl)pyruvate
2-(indol-3-yl)acetaldehyde + CO2
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-
-
-
?
3-(Indol-3-yl)pyruvate
?
-
key enzyme for indole-3-acetic acid biosynthesis
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-
?
3-(Indol-3-yl)pyruvate
?
-
rate-limiting step in the indole-3-pyruvic acid pathway
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-
?
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
3-(Indol-3-yl)pyruvate
?
-
key enzyme for indole-3-acetic acid biosynthesis
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-
?
3-(Indol-3-yl)pyruvate
?
-
rate-limiting step in the indole-3-pyruvic acid pathway
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
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0.1 mM, 8fold increase in activity. 39fold increase in activity in presence of 0.1 mM thiamine diphosphate and 5 mM Mg2+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
5 mM, 10fold increase in activity. 39fold increase in activity in presence of 0.1 mM thiamine diphosphate and 5 mM Mg2+. One of the roles of Mg2+ is to facilitate the binding of thiamin diphosphate to the enzyme by formation of a thiamine diphosphate complex
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UW5, previously misidentified as Pseudomonas putida and strain J3, J35, J51, and J55
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in a mutant lacking IpdC activity, the level of substrate indole-3-pyruvate is 2.3fold higher and the level of indole-3-lactic acid is 2.1fold higher. Phenylalanine metabolism is impacted by the loss of IpdC in the mutant strain as well as glucosinolate biosynthesis pathway
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
at pH-values between pH 5.6 and 6.0 the tetrameric form dominates, at pH values above 8.0, the monomeric form is present
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tyrR insertional mutant
activity of tyrR in Enterobacter cloacae UW5 is abolished by insertion of a tetracycline resistance cassette into the coding sequence, creating Enterobacter cloacae J35
E52D
-
decrease in Km-value for 3-(indol-3-yl)pyruvate and pyruvate, increase in Km-value for benzoylformic acid
H115K
-
slight increase in Km-value for 3-(indol-3-yl)pyruvate and pyruvate, decrease in Km-value for benzoylformic acid
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
24 h, in presence of 1 mM thiamine diphosphate and 5 mM MgCl2, stable
50
-
30 min, in presence of 1 mM thiamine diphosphate and 5 mM MgCl2, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression from the IpdC promoter and production of indole-3-acetic acid are downregulated by valine, leucine and isoleucine
expression is upregulated by the transcription factor TyrR in response to aromatic amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koga, J.; Adachi, T.; Hidaka, H.
Purification and characterization of indolepyruvate decarboxylase: A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae
J. Biol. Chem.
267
15823-15828
1992
Enterobacter cloacae
Koga, J.
Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis
Biochim. Biophys. Acta
1249
1-13
1995
Enterobacter cloacae
Schutz, A.; Sandalova, T.; Ricagno, S.; Hubner, G.; Konig, S.; Schneider, G.
Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid
Eur. J. Biochem.
270
2312-2321
2003
Enterobacter cloacae
Schutz, A.; Golbik, R.; Tittmann, K.; Svergun, D.I.; Koch, M.H.; Hubner, G.; Konig, S.
Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway
Eur. J. Biochem.
270
2322-2331
2003
Enterobacter cloacae
Schutz, A.; Golbik, R.; Konig, S.; Hubner, G.; Tittmann, K.
Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on wild-type indolepyruvate decarboxylase and variants using indolepyruvate, benzoylformate, and pyruvate as substrates
Biochemistry
44
6164-6179
2005
Enterobacter cloacae
Ryu, R.J.; Patten, C.L.
Aromatic amino acid-dependent expression of indole-3-pyruvate decarboxylase is regulated by TyrR in Enterobacter cloacae UW5
J. Bacteriol.
190
7200-7208
2008
Enterobacter cloacae (P23234), Enterobacter cloacae
Romasi, E.F.; Lee, J.
Development of indole-3-acetic acid-producing Escherichia coli by functional expression of IpdC, AspC, and Iad1
J. Microbiol. Biotechnol.
23
1726-1736
2013
Enterobacter cloacae, Enterobacter cloacae ATCC 13047
Parsons, C.; Harris, D.; Patten, C.
Regulation of indole-3-acetic acid biosynthesis by branched-chain amino acids in Enterobacter cloacae UW5
FEMS Microbiol. Lett.
362
fnv153
2015
Enterobacter cloacae (Q9FDC2), Enterobacter cloacae, Enterobacter cloacae UW5 (Q9FDC2)
Harris, D.; Berrue, F.; Kerr, R.; Patten, C.
Metabolomic analysis of indolepyruvate decarboxylase pathway derivatives in the rhizobacterium Enterobacter cloacae
Rhizosphere
6
98-111
2018
Enterobacter cloacae (Q9FDC2), Enterobacter cloacae UW5 (Q9FDC2)
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