Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WMK5

for references in articles please use BRENDA:EC4.1.3.39
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.39 4-hydroxy-2-oxovalerate aldolase
IUBMB Comments
Requires Mn2+ for maximal activity . The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH . In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase [4,5].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WMK5
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
4-hydroxy-2-oxovalerate aldolase, 4-hydroxy-2-ketovalerate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)
Requires Mn2+ for maximal activity [1]. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH [1]. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase [4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
37325-52-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
show the reaction diagram
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
show the reaction diagram
-
-
-
?
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)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
show the reaction diagram
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
the specific activity is highest with Mn2+ (100%)
additional information
not stimulated by Ca2+, Cd2+, Zn2+, and Cu2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HsaG
the enzyme is active only in complex with the dehydrogenase HsaG
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0048
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.0044
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.38
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C
0.41
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
79.1
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
93.1
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
2 * 38000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 38000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with HsaG, sitting drop vapor diffusion method, using 18% (w/v) PEG 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.5, 10% glycerol, and 10 mM sodium oxalate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carere, J.; McKenna, S.E.; Kimber, M.S.; Seah, S.Y.
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis
Biochemistry
52
3502-3511
2013
Mycobacterium tuberculosis (P9WMK5), Mycobacterium tuberculosis H37Rv (P9WMK5)
Manually annotated by BRENDA team