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Literature summary for 1.1.1.47 extracted from

  • Qian, W.; Ou, L.; Li, C.; Pan, J.; Xu, J.; Chen, Q.; Zheng, G.
    Evolution of glucose dehydrogenase for cofactor regeneration in bioredox processes with denaturing agents (2020), ChemBioChem, 21, 2680-2688 .
    View publication on PubMed
Search for more literature for 1.1.1.47

Application

Application Comment Organism
synthesis glucose dehydrogenase is a general tool for driving nicotinamide (NAD(P)H) regeneration in synthetic biochemistry. Coupled with a Candida glabrata carbonyl reductase, the mutant glucose dehydrogenase Q252L/E170K/S100P/K166R/V72I/K137R is successfully used for the asymmetric reduction of deactivating ethyl 2-oxo-4-phenylbutyrate with total turnover number of 1800 for the nicotinamide cofactor, thus making it attractive for commercial application Priestia megaterium

Protein Variants

Protein Variants Comment Organism
Q252L/E170K kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/K166R kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/S100P kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/S100P/K166R kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/S100P/K166R/K137R kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/S100P/K166R/V72I kinetic parameters of the mutant enzyme are determined Priestia megaterium
Q252L/E170K/S100P/K166R/V72I/K137R the mutant enzyme exhibits a 9.2fold increase in tolerance against 10% (v/v) 1-phenylethanol and is more stable than mutant enzyme Q252L/E170K (BmGDHM0) when exposed to hydrophobic and enzyme-inactivating compounds such as acetophenone, ethyl 2-oxo-4-phenylbutyrate, and ethyl (R)-2-hydroxy-4-phenylbutyrate Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
14.8
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P Priestia megaterium
16
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R Priestia megaterium
16.4
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R Priestia megaterium
17.2
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I Priestia megaterium
17.3
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R Priestia megaterium
17.4
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K Priestia megaterium
17.5
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R Priestia megaterium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + NAD(P)+ Priestia megaterium
-
 D-glucono-1,5-lactone + NAD(P)H + H+
-
 ?
D-glucose + NAD(P)+ Priestia megaterium IWG3
-
 D-glucono-1,5-lactone + NAD(P)H + H+
-
 ?

Organic Solvent Stability

Organic Solvent Comment Organism
1-phenylethanol mutant enzymes Q252L/E170K/S100P and Q252L/E170K/K166R display a 2.9fold and 2.0fold improvement in tolerance against 1-phenylethanol, respectively, compared with mutant enzyme Q252L/E170K. The half-life (t1/2) of mutant enzyme Q252L/E170K/S100P/K166R in the presence of 10% (v/v) 1-phenylethanol is prolonged from 70.4 min to 319 min, representing a 4.5fold increase compared with mutant enzyme Q252L/E170K. The chemical tolerance of mutant enzyme Q252L/E170K/S100P/K166R/V72I and mutant enzyme Q252L/E170K/S100P/K166R/K137R against 10% (v/v) 1-phenylethanol is increased by 5.6fold and 6.7fold, respectively, compared with mutant enzyme Q252L/E170K Priestia megaterium
acetophenone mutant enzyme Q252L/E170K retains 8% of initial activity when incubated for 12 h with 10% acetophenone Priestia megaterium
DMSO mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) DMSO Priestia megaterium
Methanol mutant enzyme Q252L/E170K maintains more than 90% of its initial activity after incubation for 24 h at 30°C with 10% (v/v) metanol Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium P40288
-
-
Priestia megaterium IWG3 P40288
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
167
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R Priestia megaterium
167
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P Priestia megaterium
169
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R Priestia megaterium
172
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K Priestia megaterium
172
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R Priestia megaterium
227
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I Priestia megaterium
239
-
 substrate: D-glucose, pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NAD(P)+
-
 Priestia megaterium D-glucono-1,5-lactone + NAD(P)H + H+
-
 ?
D-glucose + NAD(P)+
-
 Priestia megaterium IWG3 D-glucono-1,5-lactone + NAD(P)H + H+
-
 ?

Subunits

Subunits Comment Organism
homotetramer a significant hydrogen bond network is formed between the residue R166 of subunit A and E148 of both subunits A and B in mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R. In the homotetramer structure of wild-type enzyme BmGDH, the same interactions occur between subunit C (R166) and subunit D (E148) Priestia megaterium

Synonyms

Synonyms Comment Organism
GDH
-
 Priestia megaterium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
81.9
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R Priestia megaterium
82.4
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R Priestia megaterium
82.6
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P Priestia megaterium
84.4
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K Priestia megaterium
89.6
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R Priestia megaterium
112
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I Priestia megaterium
119
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R Priestia megaterium

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.7
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R Priestia megaterium
4.9
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K Priestia megaterium
5
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R Priestia megaterium
5.6
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P Priestia megaterium
5.6
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R Priestia megaterium
6.5
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I Priestia megaterium
6.9
-
 D-glucose pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R Priestia megaterium