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Literature summary for 1.1.1.261 extracted from

  • Han, J.S.; Ishikawa, K.
    Active site of Zn(2+)-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1 (2005), Archaea, 1, 311-317.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.261

Protein Variants

Protein Variants Comment Organism
D144A lower activity compared to the wild type enzyme Aeropyrum pernix
D144N lower activity compared to the wild type enzyme Aeropyrum pernix
D191N lower activity compared to the wild type enzyme Aeropyrum pernix
D191N/H271A lower activity compared to the wild type enzyme Aeropyrum pernix
H271A lower activity compared to the wild type enzyme Aeropyrum pernix
H287A lower activity compared to the wild type enzyme Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.036
-
 NADH mutant enzyme H287A Aeropyrum pernix
0.039
-
 NADPH mutant enzyme D144A Aeropyrum pernix
0.0477
-
 NADH wild type enzyme Aeropyrum pernix
0.05
-
 dihydroxyacetone phosphate wild type enzyme, with NADPH as coenzyme Aeropyrum pernix
0.086
-
 NADPH wild type enzyme Aeropyrum pernix
0.165
-
 NADPH mutant enzyme D144N Aeropyrum pernix
0.177
-
 dihydroxyacetone phosphate wild type enzyme, with NADH as coenzyme Aeropyrum pernix
0.213
-
 NADH mutant enzyme D144A Aeropyrum pernix
0.218
-
 dihydroxyacetone phosphate mutant enzyme D144A, with NADPH as coenzyme Aeropyrum pernix
0.259
-
 dihydroxyacetone phosphate mutant enzyme H287A, with NADH as coenzyme Aeropyrum pernix
0.296
-
 NADH mutant enzyme D191N Aeropyrum pernix
0.321
-
 NADH mutant enzyme H271A Aeropyrum pernix
0.36
-
 dihydroxyacetone phosphate mutant enzyme D144N, with NADPH as coenzyme Aeropyrum pernix
0.415
-
 NADH mutant enzyme D144N Aeropyrum pernix
0.633
-
 dihydroxyacetone phosphate mutant enzyme D191N, with NADH as coenzyme Aeropyrum pernix
1.09
-
 dihydroxyacetone phosphate mutant enzyme H271A, with NADH as coenzyme Aeropyrum pernix
1.12
-
 dihydroxyacetone phosphate mutant enzyme D144A, with NADH as coenzyme Aeropyrum pernix
1.12
-
 dihydroxyacetone phosphate mutant enzyme D144N, with NADH as coenzyme Aeropyrum pernix

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the specific activity abruptly increases until 0.5 mM ZnCl2 is added, and it is suppressed in the wild type when the ZnCl2 concentration exceeds 1.0 mM Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-

Storage Stability

Storage Stability Organism
4°C, 50 mM Tris-HCl buffer (pH 8.0) containing ZnCl2, 1 h, no loss of activity Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate + NAD(P)H
-
 Aeropyrum pernix sn-glycerol-1-phosphate + NAD(P)+
-
 r
sn-glycerol-1-phosphate + NAD+
-
 Aeropyrum pernix dihydroxyacetone phosphate + NADH
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Aeropyrum pernix

Synonyms

Synonyms Comment Organism
Gro1PDH
-
 Aeropyrum pernix
Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase
-
 Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
96
-
-
 Aeropyrum pernix

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.493
-
 dihydroxyacetone phosphate mutant enzyme H271A Aeropyrum pernix
1.1
-
 dihydroxyacetone phosphate mutant enzyme D144A Aeropyrum pernix
2.945
-
 dihydroxyacetone phosphate mutant enzyme H287A Aeropyrum pernix
3 6 dihydroxyacetone phosphate mutant enzyme H287A Aeropyrum pernix
3.27
-
 dihydroxyacetone phosphate mutant enzyme D191N Aeropyrum pernix
3.3
-
 dihydroxyacetone phosphate wild type enzyme Aeropyrum pernix
4.998
-
 dihydroxyacetone phosphate wild type enzyme Aeropyrum pernix
8
-
 dihydroxyacetone phosphate mutant enzyme D144N Aeropyrum pernix
18.77
-
 dihydroxyacetone phosphate mutant enzyme D144A Aeropyrum pernix
60.47
-
 dihydroxyacetone phosphate mutant enzyme D144N Aeropyrum pernix

Cofactor

Cofactor Comment Organism Structure
NAD(P)H
-
 Aeropyrum pernix