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

BRENDA support

4.1.2.55: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase

This is an abbreviated version!
For detailed information about 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase, go to the full flat file.

Word Map on EC 4.1.2.55

Reaction

2-dehydro-3-deoxy-6-phospho-D-galactonate
=
pyruvate
+
D-glyceraldehyde 3-phosphate

Synonyms

2-keto-3-deoxy-6-phosphogluconate aldolase, 2-keto-3-deoxygluconate aldolase, KD(P)G-aldolase, KDG aldolase, KDG-aldolase, KDGA, SacKdgA

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.55 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase

Crystallization

Crystallization on EC 4.1.2.55 - 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop diffusion method, three crystal forms: orthorhombic crystals of space group P2(1)2(1)2(1), which diffract to beyond 2.15 A, monoclinic crystals of space group C2, which diffract to 2.2 A, and cubic crystals of space group P4(2)32, which diffract to 3.4 A
in complex with 2-dehydro-3-deoxy-6-phospho-D-gluconate, vapor diffusion method
trapping of Schiff base complexes with natural substrates pyruvate, 2-dehydro-3-deoxy-D-gluconate, 2-dehydro-3-deoxy-D-galactonate and pyruvate plus D-glyceraldehyde at physiological pH by rapid soaking at low temperature followed by flash freezing prior to X-ray data collection. The complexes explain the substrate promiscuity of the enzyme with a rigid ligand-binding site able to accommodate both 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate
X-ray crystallographic analysis of the active site of the aldolase bound to pyruvate, 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at 4°C, reveals that its catalytic mechanism is typical of the N-acetylneuraminic acid lyase superfamily
hanging-drop method, the enzyme crystallizes in two space groups, P3(1)21 and P6(5)22, for which diffraction data are obtained to a maximum resolution of 1.8 and 2.5 A