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

BRENDA support

Literature summary for 5.3.1.1 extracted from

  • Wang, Y.; Berlow, R.B.; Loria, J.P.
    Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase (2009), Biochemistry, 48, 4548-4556.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Gallus gallus

Protein Variants

Protein Variants Comment Organism
Y208T/G210A/S211G site-directed mutagenesis Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-Glyceraldehyde 3-phosphate Gallus gallus
-
Glycerone phosphate
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glyceraldehyde 3-phosphate
-
Gallus gallus Glycerone phosphate
-
?

Subunits

Subunits Comment Organism
dimer loop-loop interactions in the dimer play a role in coordinating motions and enzymatic function in triosephosphate isomerase, NMR and circular dichroism spectroscopy structure analysis of wild-type and mutant enzymes, overview Gallus gallus

Synonyms

Synonyms Comment Organism
TIM
-
Gallus gallus
Triosephosphate isomerase
-
Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Gallus gallus