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Literature summary for 2.7.1.165 extracted from

  • Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
    Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli (1998), Biochemistry, 37, 14369-14375.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.051
-
 (R)-glycerate pH 7.5, 22°C Escherichia coli
0.061
-
 ATP pH 7.5, 22°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + (R)-glycerate Escherichia coli enzymes in the (D)-glucarate/galactarate catabolic pathway ADP + 2-phospho-(R)-glycerate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (R)-glycerate
-
 Escherichia coli ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + (R)-glycerate enzymes in the (D)-glucarate/galactarate catabolic pathway Escherichia coli ADP + 2-phospho-(R)-glycerate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5
-
 ATP pH 7.5, 22°C Escherichia coli
2.5
-
 (R)-glycerate pH 7.5, 22°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli