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

BRENDA support

Literature summary extracted from

  • Paithankar, K.S.; Feller, C.; Kuettner, E.B.; Keim, A.; Grunow, M.; Sträter, N.
    Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida (2007), FEBS J., 274, 5767-5779.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.30 enzyme expression in Escherichia coli strain XL-1 Blue Pseudomonas putida
1.1.1.30 expressed in Escherichia coli XL1-Blue cells Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.30 hanging drop vapour diffusion method with 17-20% polyethylene glycol 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2 and 10 mM acetoacetate Pseudomonas putida
1.1.1.30 recombinant enzyme, hanging drop vapor diffusion method, 0.003 ml of HBDH, 10 mg/ml, is mixed with an equal volume of crystallization buffer containing 17-20% PEG 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2, and 10 mM acetoacetate, room temperature/22°C, three different crystal forms, X-ray diffraction structure determination and analysis at resolutions between 1.9 and 2.1 A Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.30 H141A strongly decreased activity Pseudomonas putida
1.1.1.30 L149A inactive Pseudomonas putida
1.1.1.30 Q133A decreased activity Pseudomonas putida
1.1.1.30 Q91A decreased activity Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.30 0.6
-
 (R)-3-hydroxybutanoate wild type enzyme Pseudomonas putida
1.1.1.30 4
-
 (R)-3-hydroxybutanoate mutant enzyme H141A Pseudomonas putida
1.1.1.30 51
-
 (R)-3-hydroxybutanoate mutant enzyme Q91A Pseudomonas putida
1.1.1.30 70
-
 (R)-3-hydroxybutanoate mutant enzyme Q133A Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.30 (R)-3-hydroxybutanoate + NAD+ Pseudomonas putida
-
 acetoacetate + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.30 Pseudomonas putida
-
-
-
1.1.1.30 Pseudomonas putida Q9AE70
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.30 charge-controlled hydrophobic chromatography and Sephadex G-100 gel filtration Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.30 (R)-3-hydroxybutanoate + NAD+
-
 Pseudomonas putida acetoacetate + NADH
-
 r
1.1.1.30 (R)-3-hydroxybutanoate + NAD+ model of the binding mode of the substrate D-3-hydroxybutyrate, Gln193 is the only residue of the substrate-binding loop that interacts directly with the substrate, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form, overview Pseudomonas putida acetoacetate + NADH
-
 r
1.1.1.30 (R)-3-hydroxybutanoate + NAD+
-
 Pseudomonas putida acetoacetate + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.30 tetramer x-ray crystallography Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.1.1.30 D-3-hydroxybutyrate dehydrogenase
-
 Pseudomonas putida
1.1.1.30 HBDH
-
 Pseudomonas putida
1.1.1.30 More the enzyme belongs to the family of short-chain dehydrogenases/reductases Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.30 13
-
 (R)-3-hydroxybutanoate mutant enzyme H141A Pseudomonas putida
1.1.1.30 215
-
 (R)-3-hydroxybutanoate mutant enzyme Q133A Pseudomonas putida
1.1.1.30 411
-
 (R)-3-hydroxybutanoate mutant enzyme Q91A Pseudomonas putida
1.1.1.30 432
-
 (R)-3-hydroxybutanoate wild type enzyme Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.30 NAD+
-
 Pseudomonas putida
1.1.1.30 NAD+ the substrate-binding loop, residues 187-210, is partially disordered in several subunits, in both the presence and absence of NAD+, closed conformation in the complex structure with NAD+, interactions of Val185, Thr187 and Leu189 with the cosubstrate induced the conformational change from open to closed, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form Pseudomonas putida
1.1.1.30 NADH
-
 Pseudomonas putida