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Literature summary for 5.3.1.1 extracted from

  • Go, M.K.; Koudelka, A.; Amyes, T.L.; Richard, J.P.
    The role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach (2010), Biochemistry, 49, 5377-5389.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.1.1

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzyme K12G is expressed in Escherichia coli strain DF502 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
K12G the mutation results in a ca. 50fold increase in Km for the substrate glyceraldehyde 3-phosphate (GAP) and a 60fold increase in Ki for competitive inhibition by 2-phosphoglycolate, a 12000fold decrease in kcat for isomerization of GAP, and a 6000000fold decrease in kcat/Km for GAP Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
2-Phosphoglycolate competitive inhibition Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
 D-glyceraldehyde 3-phosphate wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae
50
-
 D-glyceraldehyde 3-phosphate mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate
-
 Saccharomyces cerevisiae dihydroxyacetone phosphate
-
 r

Synonyms

Synonyms Comment Organism
TIM
-
 Saccharomyces cerevisiae
Triosephosphate isomerase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.6
-
 D-glyceraldehyde 3-phosphate mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae
7300
-
 D-glyceraldehyde 3-phosphate wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
6 8
-
 Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.019
-
 2-Phosphoglycolate wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae
1.1
-
 2-Phosphoglycolate mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.012
-
 D-glyceraldehyde 3-phosphate mutant enzyme K12G, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae
6600
-
 D-glyceraldehyde 3-phosphate wild type enzyme, in 30 mM TEA at pH 7.5, at 25°C Saccharomyces cerevisiae