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Literature summary for 3.5.99.6 extracted from

  • Lara-Gonzalez, S.; Dixon, H.B.; Mendoza-Hernandez, G.; Altamirano, M.M.; Calcagno, M.L.
    On the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli (2000), J. Mol. Biol., 301, 219-227.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
N-acetylglucosamine 6-phosphate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information comparison of KM of unmodified and N-terminal modified enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A759
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification enzyme is chemically transaminated, modifying its N-terminal methionine residue to a 2-oxo-4-(methylthio)butyryl group, the transamination markedly reduces the affinity of the enzyme for its allosteric activator N-acetylglucosamine 6-phosphate, in contrast with the unmodified enzyme, which behaves as a typical allosteric K-enzyme, the modified enzyme becomes a mixed K-V allosteric protein, borohydride reduction to obtain the corresponding enzyme with a terminal hydroxy group, this enzyme shows significant recovery of the catalytic catalytic activity and its allosteric activation pattern, becomes similar to that found for the unmodified enzyme Escherichia coli
side-chain modification the modification by diethyl dicarbonate results in complete inactivation of enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-fructose 6-phosphate + NH3
-
?

Subunits

Subunits Comment Organism
hexamer
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information comparison of kcat of unmodified and N-terminal modified enzyme Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
effect of pH on homotropic co-operativity in the native and modified deaminases Escherichia coli