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Literature summary for 5.3.1.1 extracted from

  • Hernandez-Alcantara, G.; Rodriguez-Romero, A.; Reyes-Vivas, H.; Peon, J.; Cabrera, N.; Ortiz, C.; Enriquez-Flores, S.; De la Mora-De la Mora, I.; Lopez-Velazquez, G.
    Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia (2008), Biochim. Biophys. Acta, 1784, 1493-1500.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of intrinsic fluorescence of wild-type and mutants lacking Trp residues, interpretation based on crystal structure. Fluorescence of all Trp residues is quenched by aromatic-aromatic interactions due to the proximity and orientation of the indole groups of Trp196 and Tro162. Quenching is also due to energy transfer to the charged resiudes that surround Trp75, Trp173, and Trp196 Giardia intestinalis

Protein Variants

Protein Variants Comment Organism
F12W mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W162F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W162F/W173F/W196F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W173F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W196F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W75F mutant constructed for fluorescence quenching studies, catalytic properties similar to wild-type Giardia intestinalis
W75F/W162F/W173F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W75F/W162F/W196F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis
W75F/W173F/W196F mutant constructed for fluorescence studies, catalytic properties similar to wild-type Giardia intestinalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
D-glyceraldehyde 3-phosphate mutant W162F Giardia intestinalis
0.43
-
D-glyceraldehyde 3-phosphate mutant W196F Giardia intestinalis
0.6
-
D-glyceraldehyde 3-phosphate mutant F12W Giardia intestinalis
0.73
-
D-glyceraldehyde 3-phosphate mutant W75F/W162F/W196F Giardia intestinalis
0.74
-
D-glyceraldehyde 3-phosphate mutant W75F Giardia intestinalis
0.78
-
D-glyceraldehyde 3-phosphate wildtype Giardia intestinalis
0.94
-
D-glyceraldehyde 3-phosphate mutant W173F Giardia intestinalis
1
-
D-glyceraldehyde 3-phosphate mutant W162F/W173F/W196F Giardia intestinalis
1.12
-
D-glyceraldehyde 3-phosphate mutant W75F/W162F/W173F Giardia intestinalis
1.9
-
D-glyceraldehyde 3-phosphate mutant W75F/W173F/W196F Giardia intestinalis

Organism

Organism UniProt Comment Textmining
Giardia intestinalis P36186
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate
-
Giardia intestinalis dihydroxyacetone phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3166
-
D-glyceraldehyde 3-phosphate mutant W162F/W173F/W196F Giardia intestinalis
3333
-
D-glyceraldehyde 3-phosphate mutant W162F Giardia intestinalis
3666
-
D-glyceraldehyde 3-phosphate mutant W75F/W162F/W173F Giardia intestinalis
4166
-
D-glyceraldehyde 3-phosphate mutant W196F Giardia intestinalis
4333
-
D-glyceraldehyde 3-phosphate mutant W75F/W173F/W196F Giardia intestinalis
5500
-
D-glyceraldehyde 3-phosphate mutant F12W Giardia intestinalis
6166
-
D-glyceraldehyde 3-phosphate mutant W173F Giardia intestinalis
7166
-
D-glyceraldehyde 3-phosphate mutant W75F/W162F/W196F Giardia intestinalis
7666
-
D-glyceraldehyde 3-phosphate wildtype Giardia intestinalis
8000
-
D-glyceraldehyde 3-phosphate mutant W75F Giardia intestinalis