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2.4.1.14: sucrose-phosphate synthase

This is an abbreviated version!
For detailed information about sucrose-phosphate synthase, go to the full flat file.

Word Map on EC 2.4.1.14

Reaction

UDP-alpha-D-glucose
+
D-fructose 6-phosphate
=
UDP
+
sucrose 6F-phosphate

Synonyms

At5g20280, AtSPS, More, SPS, SPS A, SPS1, SPS11, Sps2, SPS4, SPS6, SPS8, SPSA, SpsB, SPSII, sucrose 6-phosphate synthase, sucrose phosphate synthase, sucrose phosphate synthase 4, sucrose phosphate synthase A, sucrose phosphate synthase B, sucrose phosphate synthetase, sucrose phosphate-uridine diphosphate glucosyltransferase, sucrose-P synthase, sucrose-phosphate synthase B, sucrosephosphate-UDP glucosyltransferase, UDP-glucose-fructose-phosphate glucosyltransferase, UDP-glucose:D-fructose-6-phosphate 2-alpha-D-glucosyltransferase, uridine diphosphoglucose-fructose phosphate glucosyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.14 sucrose-phosphate synthase

Crystallization

Crystallization on EC 2.4.1.14 - sucrose-phosphate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion technique at 25°C. Crystal structure of SPS and its complexes with the substrate D-fructose 6-phosphate and the product D-sucrose-6'-phosphate. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate D-fructose 6-phosphate and the product D-fructose 6'-phosphate bind to the A-domain of SPS. Halothermothrix orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme
spsA protein crystallized in the monocyclic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 103.16°, using hanging-drop vapour-diffusion method. Crystals diffract X-rays to a resolution limit of 3.01 A
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