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

BRENDA support

Literature summary for 4.2.1.136 extracted from

  • Shumilin, I.A.; Cymborowski, M.; Chertihin, O.; Jha, K.N.; Herr, J.C.; Lesley, S.A.; Joachimiak, A.; Minor, W.
    Identification of unknown protein function using metabolite cocktail screening (2012), Structure, 20, 1715-1725.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.136

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant protein Tm0922, hanging drop method, 1:1 mixture of a solution containing 25 mg/ml protein and 10 mM ATP with the crystallization buffer composed of 13.5% v/v PEG 400, 0.09 M MgCl2, 5% glycerol, and 0.045 M HEPES, pH 7.5, crystal soaking with metabolite cocktails, X-ray diffraction structure determination and analysis at 2.05-2.8 A resolution, analysis of the PF01256 site Thermotoga maritima
purified recombinant protein YxkO, hanging drop method, 1:1 mixture of a solution containing 25 mg/ml protein and 10 mM ATP with the crystallization buffer composed of 13.5% v/v PEG 400, 0.09 M MgCl2, 5% glycerol and 0.045 M HEPES, pH 7.5, crystal soaking with metabolite cocktails, X-ray diffraction structure determination and analysis at 1.5-1.9 A resolution, analysis of the PF01256 site Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, binding structure, overview Thermotoga maritima
Mg2+ required, binding structure, overview Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P94368
-
-
Thermotoga maritima Q9X024
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
 Thermotoga maritima AMP + phosphate + NADH
-
 ?
ADP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
 Bacillus subtilis AMP + phosphate + NADH
-
 ?
ADP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
 Thermotoga maritima AMP + phosphate + NADPH
-
 ?
ADP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
 Bacillus subtilis AMP + phosphate + NADPH
-
 ?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
 Thermotoga maritima ADP + phosphate + NADH
-
 ?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
 Bacillus subtilis ADP + phosphate + NADH
-
 ?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
 Thermotoga maritima ADP + phosphate + NADPH
-
 ?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
 Bacillus subtilis ADP + phosphate + NADPH
-
 ?
additional information substrate binding structure, overview Bacillus subtilis ?
-
 ?
additional information the C-terminal domain of Tm0922, a PF01256 protein, from Thermotoga maritima catalyzes ADP/ATP-dependent NAD(P)H-hydrate dehydratation, substrate binding structure, overview Thermotoga maritima ?
-
 ?

Synonyms

Synonyms Comment Organism
ADP/ATP-dependent NAD(P)H-hydrate dehydratase
-
 Thermotoga maritima
ADP/ATP-dependent NAD(P)H-hydrate dehydratase
-
 Bacillus subtilis
Tm0922
-
 Thermotoga maritima
YxkO
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5
-
 assay at Bacillus subtilis
25
-
 assay at Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Thermotoga maritima
8.5
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ADP dependent on, binding structure, overview Thermotoga maritima
ADP dependent on, binding structure, overview Bacillus subtilis
ATP dependent on, binding structure, overview Thermotoga maritima
ATP dependent on, binding structure, overview Bacillus subtilis

General Information

General Information Comment Organism
evolution the enzyme belongs to the PF01256 family Thermotoga maritima
evolution the enzyme belongs to the PF01256 family Bacillus subtilis
additional information catalytic residue is D216 Bacillus subtilis
additional information catalytic residue is D431 Thermotoga maritima