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

BRENDA support

Literature summary extracted from

  • Lietzan, A.D.; Nagar, M.; Pellmann, E.A.; Bourque, J.R.; Bearne, S.L.; St Maurice, M.
    Structure of mandelate racemase with bound intermediate analogues benzohydroxamate and cupferron (2012), Biochemistry, 51, 1160-1170.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.2.2 overexpression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.2.2 purified recombinant homooctameric wild-type enzyme complexed with two analogues of the putative aci-carboxylate intermediate, benzohydroxamate and Cupferron, X-ray diffraction structure at 2.2 A resolution Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 A25V site-directed mutagenesis Pseudomonas putida
5.1.2.2 T24S site-directed mutagenesis Pseudomonas putida
5.1.2.2 V22A site-directed mutagenesis Pseudomonas putida
5.1.2.2 V22F site-directed mutagenesis Pseudomonas putida
5.1.2.2 V22I site-directed mutagenesis Pseudomonas putida
5.1.2.2 V26A site-directed mutagenesis Pseudomonas putida
5.1.2.2 V26A/V29L site-directed mutagenesis Pseudomonas putida
5.1.2.2 V26F site-directed mutagenesis Pseudomonas putida
5.1.2.2 V26L site-directed mutagenesis Pseudomonas putida
5.1.2.2 V29A site-directed mutagenesis Pseudomonas putida
5.1.2.2 V29F site-directed mutagenesis Pseudomonas putida
5.1.2.2 V29L site-directed mutagenesis Pseudomonas putida
5.1.2.2 Y54F site-directed mutagenesis Pseudomonas putida
5.1.2.2 Y54L site-directed mutagenesis Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.2.2 benzohydroxamate a reasonable mimic of the transition state and/or intermediate that chelates the active site divalent metal ion and is bound in a conformation with the phenyl ring coplanar with the hydroxamate moiety, active site binding, structure comparison with bound Cupferron, overview Pseudomonas putida
5.1.2.2 Cupferron a reasonable mimic of the transition state and/or intermediate that chelates the active site divalent metal ion and is bound in a conformation with the phenyl ring coplanar with the diazeniumdiolate moiety, active site binding, structure comparison with bound benzohydroxamate, overview Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.2.2 Mg2+ dependent on Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.2.2 (S)-mandelate Pseudomonas putida
-
(R)-mandelate
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.1.2.2 Pseudomonas putida P11444
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.2.2 recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography and dialysis Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.2 (S)-mandelate
-
Pseudomonas putida (R)-mandelate
-
?

Subunits

EC Number Subunits Comment Organism
5.1.2.2 homooctamer generated from a tetramer of dimers Pseudomonas putida
5.1.2.2 More the enzyme is composed of three distinct structural domains: an N-terminal capping domain consisting of a three-stranded beta-sheet with an antiparallel four-alpha-helix bundle, a central domain consisting of a (beta/alpha)7 beta-barrel, and a short C-terminal domain composed of external beta-strands Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.2.2 25
-
assay at Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.2.2 7.5
-
assay at Pseudomonas putida