2.7.2.15: propionate kinase
This is an abbreviated version!
For detailed information about propionate kinase, go to the full flat file.
Word Map on EC 2.7.2.15
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2.7.2.15
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l-threonine
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typhimurium
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propionyl-coa
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propionyl
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non-oxidatively
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2-ketobutyrate
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in-line
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3-hydroxypropionic
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propionaldehyde
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reuteri
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1,3-propanediol
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3-hydroxypropionaldehyde
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thermophila
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nucleotide-bound
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methylcitrate
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formate-lyase
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methanosarcina
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phosphotransacetylase
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biobased
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biotechnology
- 2.7.2.15
- l-threonine
- typhimurium
- propionyl-coa
-
propionyl
-
non-oxidatively
- 2-ketobutyrate
-
in-line
-
3-hydroxypropionic
- propionaldehyde
- reuteri
- 1,3-propanediol
- 3-hydroxypropionaldehyde
- thermophila
-
nucleotide-bound
-
methylcitrate
- formate-lyase
-
methanosarcina
- phosphotransacetylase
-
biobased
- biotechnology
Reaction
Synonyms
ackA, PduW, propionate kinase II, propionate/acetate kinase, TdcD
ECTree
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Crystallization
Crystallization on EC 2.7.2.15 - propionate kinase
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by the hanging drop method, crystals of native TdcD (2.6 A resolution), TdcD-Ap4A complex in the presence of ATP (2.0 A resolution), and TdcD-Ap4A (2.4 A resolution), Ap4A is bound at the active site pocket, Ap4A is present in an extended conformation with one adenosine moiety present in the nucleotide binding site and other in the propionate binding site
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purified enzyme in complex with ATP, GTP, or CTP, soaking of crystals in 0.1 M Bis-Tris, pH 6.5, 35% pentaerythritol ethoxylate, crystals of enzyme StTdcD in complex with phosphate, AMP, ATP, Ap4, GMP, GDP, GTP, CMP and CTP are obtained using variations of crystallization conditions reported for the unliganded enzyme, X-ray diffraction structure determination and analyis at 2.4-3.0 A resolution, molecular replacement method using a polyalanine model of the unliganded StTdcD protomer, PDB ID 2E1Y as the search model, modeling