Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.3.2 extracted from

  • de Ruyck, J.; Durisotti, V.; Oudjama, Y.; Wouters, J.
    Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography (2006), J. Biol. Chem., 281, 17864-17869.
    View publication on PubMed
Search for more literature for 5.3.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
of wild-type and mutants Y104A, Y104F Escherichia coli

Protein Variants

Protein Variants Comment Organism
Y104A 0.1% of wild-type activity. Crystallization data. The M2+ metal-binding site is absent in the structure, but Mg2+ is still present and bound to C67, E87, and four water molecules Escherichia coli
Y104F 0.1% of wild-type activity. Crystallization data. General fold of enzyme is similar to wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0095
-
 isopentenyl diphosphate wild-type, pH 7.4, 37°C Escherichia coli
0.0142
-
 isopentenyl diphosphate mutant Y104F, pH 7.4, 37°C Escherichia coli
0.0225
-
 isopentenyl diphosphate mutant Y104A, pH 7.4, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli Q46822
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isopentenyl diphosphate
-
 Escherichia coli dimethylallyl diphosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48
-
 melting temperature of mutant Y104A Escherichia coli
55
-
 melting temperature of mutant Y104F Escherichia coli
69
-
 melting temperature of wild-type Escherichia coli