5.1.3.30: D-psicose 3-epimerase
This is an abbreviated version!
For detailed information about D-psicose 3-epimerase, go to the full flat file.
Word Map on EC 5.1.3.30
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5.1.3.30
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d-fructose
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tumefaciens
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agrobacterium
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d-tagatose
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d-allulose
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clostridium
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bioconversion
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synthesis
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epimerization
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metal-dependent
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ruminococcus
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cellulolyticum
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low-calorie
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ketose
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sweetener
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reusable
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d-sorbose
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izumoring
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ketohexose
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ni-affinity
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food-grade
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low-energy
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reusability
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noncharacterized
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bolteae
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fermentor
- 5.1.3.30
- d-fructose
- tumefaciens
- agrobacterium
- d-tagatose
- d-allulose
- clostridium
-
bioconversion
- synthesis
-
epimerization
-
metal-dependent
- ruminococcus
- cellulolyticum
-
low-calorie
-
ketose
-
sweetener
-
reusable
- d-sorbose
-
izumoring
-
ketohexose
-
ni-affinity
-
food-grade
-
low-energy
-
reusability
-
noncharacterized
- bolteae
-
fermentor
Reaction
Synonyms
ACL75304 protein, CB-DPEase, Ccel_0941, Clo1100_1157, CLOBOL_00069, CLOSCI_02528, Dosp-DPEase, DPE, DPEase, DTEase, RDPE, Trpr-DPEase
ECTree
5.1.3.30 D-psicose 3-epimeraseAdvanced search results
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results (Crystallization
Crystallization on EC 5.1.3.30 - D-psicose 3-epimerase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
sitting drop method. The crystal structure of the apoenzyme and the enzyme in complex with substrates or products (D-psicose, D-fructose, D-tagatose and D-sorbose). From the complex structures of the enzyme with D-psicose and D-fructose, the enzyme has much more interactions with D-psicose than D-fructose by forming more hydrogen bonds between the substrate and the active site residues. Accordingly, based on these ketohexosebound complex structures, a C3-O3 proton-exchange mechanism for the conversion between D-psicose and D-fructose is proposed. These results provide a clear idea for the deprotonation/protonation roles of E150 and E244 in catalysis
