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Information on EC 4.1.3.43 - 4-hydroxy-2-oxohexanoate aldolase and Organism(s) Thermus thermophilus and UniProt Accession Q53WI0

for references in articles please use BRENDA:EC4.1.3.43
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.43 4-hydroxy-2-oxohexanoate aldolase
IUBMB Comments
Requires Mn2+ for maximal activity [1,2]. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase [1,2,6]. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits [3,4,6].
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q53WI0
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
tthb246, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(S)-4-hydroxy-2-oxohexanoate pyruvate-lyase (propanal-forming)
Requires Mn2+ for maximal activity [1,2]. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase [1,2,6]. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits [3,4,6].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4S)-4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
show the reaction diagram
-
-
-
?
4-hydroxy-2-oxohexanoate
propanal + pyruvate
show the reaction diagram
-
-
-
?
4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 0.218
4-hydroxy-2-oxohexanoate
0.041 - 0.295
4-hydroxy-2-oxopentanoate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 3.9
4-hydroxy-2-oxohexanoate
0.08 - 4.1
4-hydroxy-2-oxopentanoate
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 33.3
4-hydroxy-2-oxohexanoate
0.8 - 46.1
4-hydroxy-2-oxopentanoate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
together with TTHB247, EC 1.2.1.87, enzyme forms a bacterial aldolase-dehydrogenase complex catalyzing the last steps in the meta cleavage pathway of aromatic hydrocarbon degradation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
142000
native molecular mass of TTHB246-TTHB247 complex, determined by gel filtration
144000
molecular mass of TTHB246-BphJ chimeric complex, determined by gel filtration
145000
molecular mass of TTHB246-BphJ chimeric complex, determined by static light scattering
152000
native molecular mass of TTHB246-TTHB247 complex, determined by static light scattering
37000
estimated by SDS-PAGE, in agreement with predicted molecular mass calculated from amino acid sequences
72000
native molecular mass of TTHB246, determined by gel filtration
78000
native molecular mass of TTHB246, determined by static light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
enzyme can form a stable heterotetrameric complex with TTHB247 in vitro, consisting of two aldolase and two dehydrogenase subunits
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A324G
increase of channeling efficiency of propionaldehyde to a value comparable to that of acetaldehyde
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified to homogeneity using Ni2+-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric complexes of Burkholderia xenovorans and Thermus thermophilus enzymes, TTHB246-BphJ and BphI-TTHB247 created by coexpression of the relevant genes in Escherichia coli using separate expression plasmids
separate expression of TTHB246 in recombinant Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, P.; Hillis, C.; Carere, J.; Seah, S.Y.K.
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes
Biochemistry
51
1942-1952
2012
Thermus thermophilus (Q53WI0), Thermus thermophilus
Manually annotated by BRENDA team