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BRENDA support

Literature summary for 1.2.4.4 extracted from

  • Hester, K.; Luo, J.; Burns, B.; Braswell, E.H.; Sokatch, J.R.
    Purification of active E1alpha2beta2 of Pseudomonas putida branched-chain-oxoacid dehydrogenase (1995), Eur. J. Biochem., 233, 828-836.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thiamine diphosphate
-
Pseudomonas putida

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
S313A twofold increase in Km-value but no change in turnover-number Pseudomonas putida
S315A mutation has no effect on Km-value or turnover-number Pseudomonas putida
S319A mutation has no effect on Km-value or turnover-number Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
172000
-
equilibrium sedimentation Pseudomonas putida
190000
-
E1 component, gel filtration Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas putida

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
26
-
-
Pseudomonas putida
38
-
E1 component expressed in Escherichia coli Pseudomonas putida

Subunits

Subunits Comment Organism
tetramer alpha2,beta2, MW of alpha is 45000 Da, expression of bkdA2 yields the 39000 Da form and the 37000 Da form of the beta-subunit, both forms of the E1 beta-subunit are produced in Pseudomonas putida, only the 39000 Da protein is produced in Escherichia coli, SDS-PAGE Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
CoA
-
Pseudomonas putida
NAD+
-
Pseudomonas putida