Literature summary for 4.1.1.43 extracted from

Versees, W.; Spaepen, S.; Wood, M.D.; Leeper, F.J.; Vanderleyden, J.; Steyaert, J.
Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase (2007), J. Biol. Chem., 282, 35269-35278.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Azospirillum brasilense

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion method with 15% polyethylene glycol 4000 (w/v), 10% glycerol (v/v) in 100 mM HEPES buffer, pH 7.0	Azospirillum brasilense

Inhibitors

Inhibitors	Comment	Organism	Structure
2-(1-hydroxyethyl)-3-deaza-thiamine diphosphate	-	Azospirillum brasilense
3-deaza-thiamine diphosphate	-	Azospirillum brasilense

Organism

Organism	UniProt	Comment	Textmining
Azospirillum brasilense	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Azospirillum brasilense

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
indolepyruvate	-	Azospirillum brasilense	indoleacetaldehyde + CO2	-	?
L-phenylalanine	-	Azospirillum brasilense	phenylacetic acid + CO2	-	?
L-tryptophan	-	Azospirillum brasilense	indole-acetic acid + CO2	-	?
Phenylpyruvate	-	Azospirillum brasilense	Phenylacetaldehyde + CO2	-	?

Subunits

Subunits	Comment	Organism
homotetramer	X-ray crystallography, in solution	Azospirillum brasilense

Synonyms

Synonyms	Comment	Organism
PPDC	-	Azospirillum brasilense

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	dependent	Azospirillum brasilense

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Release 2023.1 (January 2023)