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Literature summary for 4.2.1.2 extracted from

  • Estevez, M.; Skarda, J.; Spencer, J.; Banaszak, L.; Weaver, T.M.
    X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation (2002), Protein Sci., 11, 1552-1557.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme E315Q Escherichia coli

Protein Variants

Protein Variants Comment Organism
E315Q mutation causes about 3% increase in Km-value for S-malate, about 20% increase in Km-value for fumarate. 10fold decrease in turnover number for S-malate, about 11fold decrease in turnover number for fumarate Escherichia coli
additional information E319Q mutation, an inborn error of fumarase causes progressive psychomotor retardation, failure to thrive, microcephaly and abnormal posture with hypotonia contrasting with hypertonia of limbs Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
fumarate + H2O Homo sapiens enzyme of Krebs cycle L-malate
-
r
fumarate + H2O Escherichia coli enzyme of Krebs cycle L-malate
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P05042
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + H2O
-
Homo sapiens L-malate
-
r
fumarate + H2O
-
Escherichia coli L-malate
-
r
fumarate + H2O enzyme of Krebs cycle Homo sapiens L-malate
-
r
fumarate + H2O enzyme of Krebs cycle Escherichia coli L-malate
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
L-malate pH 7.9, mutant enzyme E315Q Escherichia coli
1149
-
fumarate pH 7.9, native enzyme Escherichia coli
1150
-
fumarate pH 7.9, native enzyme Escherichia coli