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

BRENDA support

Literature summary for 1.1.1.384 extracted from

  • Kubiak, R.L.; Holden, H.M.
    Combined structural and functional investigation of a C-3''-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose (2011), Biochemistry, 50, 5905-5917.
    View publication on PubMed
Search for more literature for 1.1.1.384

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Actinomadura kijaniata

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method of vapor diffusion, binary and ternary complexes of KijD10 with NADP+ and dTDP-benzene, 2.0 A resolution or better Actinomadura kijaniata

Protein Variants

Protein Variants Comment Organism
K102A mutant protein is completely inactive Actinomadura kijaniata
K102E mutant enzyme retains some activity, but its catalytic efficiency is reduced by more than 4 orders of magnitude from that for the wild-type enzyme Actinomadura kijaniata
K102M mutant protein is completely inactive Actinomadura kijaniata
K102Q mutant protein is completely inactive Actinomadura kijaniata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data are determined for mutant enzymes and wild-type enzyme Actinomadura kijaniata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+ Actinomadura kijaniata the enzyme is involved in the biosynthesis of dTDP-L-digitoxose dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Actinomadura kijaniata B3TMR8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Actinomadura kijaniata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+ the enzyme is involved in the biosynthesis of dTDP-L-digitoxose Actinomadura kijaniata dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
 ?
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+ dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose =(2R,6S)-6-hydroxy-2-methyldihydro-2H-pyran-3,4-dione Actinomadura kijaniata dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+ dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose = dTDP-2,6-dideoxy-alpha-D-threo-hexopyranos-4-ulose ?
dTDP-3-dehydro-6-deoxy-alpha D-galactose + NADPH + H+
-
 Actinomadura kijaniata dTDP-fucose + NADP+
-
 ?
dTDP-3-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
 Actinomadura kijaniata dTDP-quinovose + NADP+
-
 ?
additional information to functioning on its natural substrate, KijD10 can also turn over sugars that contain hydroxyl groups at the C-2 and C-4 positions. It does not discriminate with respect to the orientation of the hydroxyl group at C-4 Actinomadura kijaniata ?
-
 ?

Synonyms

Synonyms Comment Organism
KijD10
-
 Actinomadura kijaniata

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Actinomadura kijaniata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data are determined for mutant enzymes and wild-type enzyme Actinomadura kijaniata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Actinomadura kijaniata

General Information

General Information Comment Organism
physiological function the enzyme is involved in the biosynthesis of dTDP-L-digitoxose Actinomadura kijaniata

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information kinetic data are determined for mutant enzymes and wild-type enzyme Actinomadura kijaniata