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Information on EC 4.1.1.5 - acetolactate decarboxylase and Organism(s) Streptococcus thermophilus and UniProt Accession Q8L208

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.5 acetolactate decarboxylase
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This record set is specific for:
Streptococcus thermophilus
UNIPROT: Q8L208 not found.
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Word Map
The taxonomic range for the selected organisms is: Streptococcus thermophilus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
alpha-acetolactate decarboxylase, acetolactate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ALDC
-
-
-
-
alpha-Acetolactate decarboxylase
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-
-
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Decarboxylase, acetolactate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(3R)-3-hydroxybutan-2-one-forming]
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-02-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2-hydroxy-2-methyl-3-oxobutanoate
(R)-acetoin + CO2
show the reaction diagram
regulates leucine and valine biosynthesis by diverting the flux of alpha-acetolactate towards acetoin when branched-chain amino acids are present at a high concentration, involved in catabolism of pyruvate to acetoin, but less important function in vivo
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
isoleucine
requirement for branched-chain amino acids, control of the pool of alpha-acetolactate by valine, leucine and isoleucine via allosteric activation, valine is more stimulatory than leucine and isoleucine
leucine
requirement for branched-chain amino acids, control of the pool of alpha-acetolactate by valine, leucine and isoleucine via allosteric activation, valine is more stimulatory than leucine and isoleucine
valine
requirement for branched-chain amino acids, control of the pool of alpha-acetolactate by valine, leucine and isoleucine via allosteric activation, valine is more stimulatory than leucine and isoleucine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
culture in the presence of leucine and isoleucine
0.472
culture in the presence of leucine and valine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALDC_STRTR
239
0
26843
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
aldC gene, expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Monnet, C.; Nardi, M.; Hols, P.; Gulea, M.; Corrieu, G.; Monnet, V.
Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase in Streptococcus thermophilus
Lett. Appl. Microbiol.
36
399-405
2003
Streptococcus thermophilus (Q8L208), Streptococcus thermophilus, Streptococcus thermophilus CNRZ385 (Q8L208), Streptococcus thermophilus CNRZ385
Manually annotated by BRENDA team