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Literature summary for 4.1.2.14 extracted from

  • 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 (2018), Appl. Microbiol. Biotechnol., 102, 8359-8372 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + D-glyceraldehyde 3-phosphate Escherichia coli
-
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A955
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + D-glyceraldehyde 3-phosphate
-
Escherichia coli 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
?
pyruvate + glyoxylate
-
Escherichia coli (4S)-4-hydroxy-2-oxoglutarate
-
r

Synonyms

Synonyms Comment Organism
2-oxo-3-deoxy-6-phosphogluconate aldolase
-
Escherichia coli
eda
-
Escherichia coli
KDPGlc aldolase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Escherichia coli