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

BRENDA support

4.1.2.14: 2-dehydro-3-deoxy-phosphogluconate aldolase

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

Word Map on EC 4.1.2.14

Reaction

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

Synonyms

2-dehydro-3-deoxy-phosphogluconate aldolase, 2-dehydro-3-deoxyphosphogluconate aldolase, 2-keto-3-deoxy-(6-phospho)-gluconate aldolase, 2-keto-3-deoxy-6-phosphogluconate aldolase, 2-keto-3-deoxy-6-phosphogluconic aldolase, 2-keto-3-deoxygluconate-6-P-aldolase, 2-keto-3-deoxygluconate-6-phosphate aldolase, 2-oxo-3-deoxy-6-phosphogluconate aldolase, 6-phospho-2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-3-phosphate-lyase, 6-Phospho-2-keto-3-deoxygluconate aldolase, aldolase, phospho-2-keto-3-deoxygluconate, eda, KD(P)G aldolase, KDGA, KDPG aldolase, KDPG-aldolase, KDPGA, KDPGlc aldolase, ODPG aldolase, Phospho-2-dehydro-3-deoxygluconate aldolase, Phospho-2-keto-3-deoxygluconate aldolase, Phospho-2-keto-3-deoxygluconic aldolase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.14 2-dehydro-3-deoxy-phosphogluconate aldolase

Engineering

Engineering on EC 4.1.2.14 - 2-dehydro-3-deoxy-phosphogluconate aldolase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E9K/V118A
-
KA1-4 variant, improved cleavage of D-2-dehydro-deoxygluconate
G40A/V188A
-
KA1-1 variant, improved cleavage of D-2-dehydro-deoxygluconate
K133Q
no aldolase activity
K133Q/T161K
reduced catalytic efficiency
S184A
-
the mutation decreases the efficiency of KDPG retro-aldol cleavage only modestly
S184D
-
the mutation leads to strongly reduced enzymatic activity
S184F
-
active site mutation, enhances the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
S184L
-
the mutation is located in the substrate-binding pocket, interacts with the phosphate moiety of KDPG, and improves the catalytic efficiency for the synthesis of a precursor for nikkomycin by 40fold
T161A
-
strongly reduced activity
T161S
-
active site mutation, enhances the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
T161S/S184F
-
active site mutation, working additively to enhance the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
T161S/S184L
-
active site mutation, working additively to enhance the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate. Mutations improve the value of kcat/KM (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate by more than 450fold, resulting in a catalytic efficiency that is comparable to that of the wild-type enzyme with the natural substrate while retaining high stereoselectivity
T161V
-
strongly reduced activity
T84A/I92F
-
KA1-2 variant, improved cleavage of D-2-dehydro-deoxygluconate
T84A/I92F/V118A
-
KA2 variant, improved kcat, Km and thermal stability
T84A/I92F/V118A/E138V
-
KA3 variant, small change of melting temperature
T84A/I92F/V118A/G141S/T105I
-
KA3-L2 variant, slightly less stable than wild-type
T84A/I92F/V118A/T161A
-
KA3-L1 variant, enhanced activity towards negatively charged glyoxylate and glyceraldehyde-3-phosphate
V118A
-
KA1-3 variant, improved cleavage of D-2-dehydro-deoxygluconate