2.3.1.8: phosphate acetyltransferase
This is an abbreviated version!
For detailed information about phosphate acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.8
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2.3.1.8
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acetyl-coenzyme
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methanosarcina
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thermophila
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formate-lyase
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acetobutylicum
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pta-ack
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acetogenic
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coash
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acka-pta
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2.7.2.1
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phosphoketolase
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acetoin
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acetate-activating
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butyryl-coa
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tyrobutyricum
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substrate-level
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2,3-butanediol
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acetate-grown
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acetylphosphate
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sulfoacetaldehyde
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synthesis
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biotechnology
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biofuel production
- 2.3.1.8
-
acetyl-coenzyme
- methanosarcina
- thermophila
- formate-lyase
- acetobutylicum
-
pta-ack
-
acetogenic
- coash
-
acka-pta
-
2.7.2.1
- phosphoketolase
- acetoin
-
acetate-activating
- butyryl-coa
- tyrobutyricum
-
substrate-level
- 2,3-butanediol
-
acetate-grown
- acetylphosphate
- sulfoacetaldehyde
- synthesis
- biotechnology
- biofuel production
Reaction
Synonyms
acetyl-S-CoA: orthophosphate acetyltransferase, acetyltransferase, phosphate, aster yellows witches'-broom phosphotransacetylase-like enzyme, AYWB-PduL, EutD, Moth_0864, Moth_1181, pduL1, pduL2, PGN_1179, phosphate acetyltransferase, phosphoacylase, phosphotransacetylase, phosphotransacetylase EutD, phosphotransacetylase Pta, PTA, Pta-1, Pta-2, PtaII1, PtaII2
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Crystallization
Crystallization on EC 2.3.1.8 - phosphate acetyltransferase
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hanging drop vapor diffusion method, crystal structures of the enzyme at 2.75 A resolution and its complex with acetyl phosphate at 2.85 A resolution
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hanging drop vapor diffusion method. Crystal structures of phosphotransacetylase in complex with the substrate CoA reveals one CoA (CoA(1)) bound in the proposed active site cleft and an additional CoA (CoA(2)) bound at the periphery of the cleft. The crystal structures indicat that binding of CoA(1) is mediated by a series of hydrogen bonds and extensive van der Waals interactions with the enzyme and that there are fewer of these interactions between CoA(2) and the enzyme
to 2.04 A resolution. An acetyl-CoA molecule binds to each subunit of the dimer