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Literature summary extracted from

  • Kim, G.; Shin, D.; Lee, S.; Yun, J.; Lee, S.
    Crystal structure of ILvC, a ketol-acid reductoisomerase, from Streptococcus pneumoniae (2019), Crystals, 9, 551 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.86 expression in Escherichia coli BL21(DE3) Streptococcus pneumoniae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.86 micro-batch and hanging-drop vapor-diffusion methods. The crystal structure is determined at 1.69 A resolution. The crystal structure of SpIlvC contains an asymmetric dimer in which one subunit is in apo-form and the other in NADP(H) and Mg2+-bound form Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.86 D191G crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 D191K mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 D83G crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 E195A mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 E195K mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 E195S crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 R49A mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 R49E crystal structure of the mutants (R49E, D83G, D191G and E195S) reveals local conformational changes only in the NADP(H) binding site. Mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 R49G mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 S53A mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 S53G mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 S53K mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae
1.1.1.86 S53T mutant enzyme exhibits significantly reduced activities compared to wild-type enzyme Streptococcus pneumoniae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.86 0.07
-
NADPH wild-type enzyme, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.199
-
NADPH mutant enzyme S53G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.33
-
NADPH mutant enzyme D83G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.345
-
NADPH mutant enzyme S53T, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.355
-
NADPH mutant enzyme D191G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.395
-
NADPH mutant enzyme R49G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.47 1 NADPH mutant enzyme S53K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.472
-
NADPH mutant enzyme R49E, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.588
-
NADPH mutant enzyme R49A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.677
-
NADPH mutant enzyme S53A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.732
-
NADPH mutant enzyme E195A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.895
-
NADPH mutant enzyme E195K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 1.036
-
NADPH mutant enzyme D191K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 1.467
-
NADPH mutant enzyme E195S, pH 8.0, 30°C Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.86 Streptococcus pneumoniae Q04M32
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.86
-
Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.86 (2S)-2-acetolactate + NADPH + H+
-
Streptococcus pneumoniae (R)-2,3-dihydroxyisovalerate + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.86 dimer the enzyme retains dimeric arrangement in solution Streptococcus pneumoniae

Synonyms

EC Number Synonyms Comment Organism
1.1.1.86 ilvC
-
Streptococcus pneumoniae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.86 0.1
-
NADPH wild-type enzyme, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.11
-
NADPH mutant enzyme S53G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.12
-
NADPH mutant enzyme D191K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.12
-
NADPH mutant enzyme E195A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.12
-
NADPH mutant enzyme S53T, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.13
-
NADPH mutant enzyme D83G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.14
-
NADPH mutant enzyme S53K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.15
-
NADPH mutant enzyme D191G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.16
-
NADPH mutant enzyme R49G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.17
-
NADPH mutant enzyme S53A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.18
-
NADPH mutant enzyme E195K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.18
-
NADPH mutant enzyme R49A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.18
-
NADPH mutant enzyme R49E, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.25
-
NADPH mutant enzyme E195S, pH 8.0, 30°C Streptococcus pneumoniae

General Information

EC Number General Information Comment Organism
1.1.1.86 metabolism the enzyme catalyzes the second step in the BCAA biosynthetic pathway Streptococcus pneumoniae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.86 0.16
-
NADPH mutant enzyme E195A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.17
-
NADPH mutant enzyme E195S, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.2
-
NADPH mutant enzyme E195K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.21
-
NADPH mutant enzyme D191K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.25
-
NADPH mutant enzyme S53A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.3
-
NADPH mutant enzyme R49A, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.3
-
NADPH mutant enzyme S53K, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.34
-
NADPH mutant enzyme S53T, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.38
-
NADPH mutant enzyme R49E, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.39
-
NADPH mutant enzyme D83G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.42
-
NADPH mutant enzyme D191G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.43
-
NADPH mutant enzyme R49G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 0.55
-
NADPH mutant enzyme S53G, pH 8.0, 30°C Streptococcus pneumoniae
1.1.1.86 1.4
-
NADPH wild-type enzyme, pH 8.0, 30°C Streptococcus pneumoniae