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Literature summary extracted from

  • Israyilova, A.; Buroni, S.; Forneris, F.; Scoffone, V.C.; Shixaliyev, N.Q.; Riccardi, G.; Chiarelli, L.R.
    Biochemical characterization of glutamate racemase - a new candidate drug target against Burkholderia cenocepacia infections (2016), PLoS ONE, 11, e0167350 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
5.1.1.3 drug development the enzyme is a good target for antibacterial drug development for treatment of Burkholderia cenocepacia infections causing cystic fibrosis Burkholderia cenocepacia

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.3 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Burkholderia cenocepacia

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.3 (2R)-2-amino-4-benzylpentanedioic acid
-
Burkholderia cenocepacia
5.1.1.3 1H-benzimidazole-2-sulfonic acid
-
Burkholderia cenocepacia
5.1.1.3 4-hydroxybenzene-1,3-disulfonate
-
Burkholderia cenocepacia
5.1.1.3 bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex binding structure, overview Burkholderia cenocepacia
5.1.1.3 Cu2+ inhibition is completely reversed by EDTA Burkholderia cenocepacia
5.1.1.3 dipicolinic acid
-
Burkholderia cenocepacia
5.1.1.3 Mn2+ inhibition is completely reversed by EDTA Burkholderia cenocepacia
5.1.1.3 additional information library screening for inhibitory compounds, two Zn (II) and Mn (III) 1,3,5-triazapentadienate complexes are found to efficiently inhibit the glutamate racemase activity. The metal complexes affect the enzyme activity by binding to the enzyme-substrate complex and promoting the formation of an inhibited dimeric form of the enzyme. Evaluation of a series of compounds, including 1H-benzimidazole-2-sulfonic acid, dipicolinic acid, 4-hydroxybenzene-1,3-disulfonate, and (2R)-2-amino-4-benzylpentanedioic acid, which are already known inhibitors of different bacterial glutamate racemases, for inhibitory activity on the enzyme, inhibition mechanism of BcGR by metal complexes, overview Burkholderia cenocepacia
5.1.1.3 tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex binding structure, overview Burkholderia cenocepacia
5.1.1.3 Zn2+ inhibition is completely reversed by EDTA Burkholderia cenocepacia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 additional information
-
additional information recombinant enzyme, steady state kinetic analysis Burkholderia cenocepacia
5.1.1.3 13.89
-
D-glutamate recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.3 additional information no effects on activity by Mg2+, Fe2+, and Ni2+ Burkholderia cenocepacia

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.3 31000
-
recombinant detagged monomeric enzyme, gel filtration Burkholderia cenocepacia
5.1.1.3 70000
-
recombinant detagged dimeric enzyme, gel filtration Burkholderia cenocepacia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.3 L-glutamate Burkholderia cenocepacia
-
D-glutamate
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Burkholderia cenocepacia
-
-
-
5.1.1.3 no activity in Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage with the PreScission protease, dialysis and another step of nickel affinity chromatography, to homogeneity Burkholderia cenocepacia

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.3 2.4
-
purified recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.3 D-glutamate
-
Burkholderia cenocepacia L-glutamate
-
r
5.1.1.3 L-glutamate
-
Burkholderia cenocepacia D-glutamate
-
r

Subunits

EC Number Subunits Comment Organism
5.1.1.3 homodimer 2 * 30000, about, SDS-PAGE Burkholderia cenocepacia

Synonyms

EC Number Synonyms Comment Organism
5.1.1.3 BcGR
-
Burkholderia cenocepacia

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.3 40 50
-
Burkholderia cenocepacia

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.1.3 37 50 maximal activity at 40-50°C, 80% activity at 37°C Burkholderia cenocepacia

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.3 40
-
purified recombinant enzyme, pH 8.0, moderately stable preserving more than 80% of initial activity after 2 h at up to 40°C, but rapidly loses all activity at higher temperatures Burkholderia cenocepacia

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.1.3 0.025
-
D-glutamate recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.3 8 9
-
Burkholderia cenocepacia

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.3 6 10 enzyme exhibits a preference for high pH values, showing an optimal activity at pH 8.0-9.0, with about 70% of maximal activity at pH 9.5, and less than 50% activity below pH 7.0 Burkholderia cenocepacia

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
5.1.1.3 6 9.5 purified recombinant enzyme, 37°C, full activity is almost preserved at pH values pH 7.0-8.5, whereas the stability dramatically decreases at pH values below pH 6.0 or up to pH 9.5, with less than 40% of the initial activity remaining Burkholderia cenocepacia

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.3 pyridoxal 5'-phosphate
-
Burkholderia cenocepacia

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
5.1.1.3 0.01
-
recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex
5.1.1.3 0.0353
-
recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex
5.1.1.3 0.15
-
recombinant enzyme, pH 8.0, 37°C Burkholderia cenocepacia dipicolinic acid

General Information

EC Number General Information Comment Organism
5.1.1.3 additional information structure homology modeling, in BcGR, all critical residues for enzymatic activity and substrate recognition are fully conserved within the 2-domain glutamate racemase fold Burkholderia cenocepacia
5.1.1.3 physiological function glutamate racemase is an essential enzyme for the biosynthesis of the bacterial cell wall Burkholderia cenocepacia