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Information on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase and Organism(s) Escherichia coli and UniProt Accession P0A955

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.16 4-Hydroxy-2-oxoglutarate aldolase
IUBMB Comments
The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, (4S)-4-hydroxy-2-oxoglutarate aldolase.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A955
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hoga1, 4-hydroxy-2-oxoglutarate aldolase, 2-keto-4-hydroxyglutarate aldolase, 2-oxo-4-hydroxyglutarate aldolase, dhdpsl, 4-hydroxy-2-ketoglutarate aldolase, entner-doudoroff aldolase, dihydrodipicolinate synthase-like enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxo-3-deoxy-6-phosphogluconate aldolase
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Entner-Doudoroff aldolase
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KDPGlc aldolase
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2-keto-4-hydroxybutyrate aldolase
-
-
-
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2-keto-4-hydroxyglutarate aldolase
-
-
-
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2-keto-4-hydroxyglutaric aldolase
-
-
-
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2-oxo-4-hydroxyglutarate aldolase
-
-
-
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2-oxo-4-hydroxyglutaric aldolase
-
-
-
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4-hydroxy-2-ketoglutarate aldolase
-
-
-
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4-hydroxy-2-ketoglutaric aldolase
-
-
-
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aldolase, 4-hydroxy-2-oxoglutarate
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-
-
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DL-4-Hydroxy-2-ketoglutarate aldolase
-
-
-
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hydroxyketoglutarate aldolase
-
-
-
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Hydroxyketoglutaric aldolase
-
-
-
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KHG-aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)
The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, (4S)-4-hydroxy-2-oxoglutarate aldolase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-81-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
show the reaction diagram
-
-
-
r
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
4-Hydroxy-2-oxoglutarate
Pyruvate + glyoxylate
show the reaction diagram
-
-
-
r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schapfl, M.; Baier, S.; Fries, A.; Ferlaino, S.; Waltzer, S.; Mueller, M.; Sprenger, G.A.
Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C-C-bonding reactions
Appl. Microbiol. Biotechnol.
102
8359-8372
2018
Escherichia coli (P0A955)
Manually annotated by BRENDA team