1.1.1.22: UDP-glucose 6-dehydrogenase

This is an abbreviated version, for detailed information about UDP-glucose 6-dehydrogenase, go to the full flat file.

Reaction

UDP-alpha-D-glucose
+ 2 NAD+ +
H2O
=
UDP-alpha-D-glucuronate
+ 2 NADH + 2 H+

Synonyms

ADH-like UDP-glucose dehydrogenase, AglM, BceC, dehydrogenase, uridine diphosphoglucose, dual specificity UDP-glucose dehydrogenase, HasB, HasB2, HVO_1531, PA2022, PA3559, sqv-4, Sugarless protein, UDP-alpha-D-glucose:NAD oxidoreductase, UDP-D-glucose dehydrogenase, UDP-GDH, UDP-Glc dehydrogenase, UDP-Glc DH, UDP-GlcDH, UDP-GlcDHase, UDP-glucose dehydrogenase, UDPDH, UDPG dehydrogenase, UDPG-DH, UDPG:NAD oxidoreductase, UDPGD, UDPGDH, UDPGDH-A, UDPGDH-B, UDPGlc dehydrogenase, UDPglucose dehydrogenase, UDPglucose:NAD+ oxidoreductase, Ugd, UGD1, UgdG, UGDH, uridine diphosphate D-glucose dehydrogenase, uridine diphosphate glucose dehydrogenase, uridine diphosphate glucose-6-dehydrogenase, uridine diphosphate-glucose dehydrogenase, uridine diphosphoglucose dehydrogenase, uridine-5'-diphosphoglucose dehydrogenase, uridyl phosphate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.22 UDP-glucose 6-dehydrogenase

Engineering

Engineering on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y10F
mutation in GXGYXG consensus motif, 9% residual activity. Tyr10 plays a catalytic role in the final hydrolysis step. Upon release of NADH after the second oxidation step, Tyr10 may work as a proton conveyer from the aqueous hydrogen-bonding proton wire system to the hydrolytic site
Y10K
mutation in GXGYXG consensus motif, 2% residual activity
Y10S
mutation in GXGYXG consensus motif, 3% residual activity
A222Q/S233G
C276E
-
activity is not measurable at pH 8.7, 22C
C276G
-
activity is not measurable at pH 8.7, 22C
C276K
-
activity is not measurable at pH 8.7, 22C
C276L
-
activity is not measurable at pH 8.7, 22C
C276Y
-
activity is not measurable at pH 8.7, 22C
D280A
-
extremely poor enzymic activity
D280E
-
site-directed mutagenesis, 3-fold increase in Km for UDP-glucose and a 2-fold reduced Vmax relative to that of the wild type
DELTA132
-
deletion of residue Val132 from the Thr131 loop to approximate an intermediate state in the allosteric transition. The crystal structure of the deletion construct reveals an open conformation that relaxes steric constraints and facilitates repacking of the protein core. The open conformation stabilizes the construct as a hexamer with point group symmetry 32, similar to that of the active complex. The DELTA132 and UDP-alpha-D-xylose-inhibited structures have similar hexamer-building interfaces
E161Q
-
hydrolysis step becomes completely rate-limiting so that a thioester enzyme intermediate accumulates at steady state. Crystallization of E161Q in the presence of 5 mM UDP-glucose and 2 mM NAD results in trapping a thiohemiacetal enzyme intermediate
G13E
normal expression and stability of mutant, no enzymic activity, no photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
K220H
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
K220R
-
site-directed mutagenesis, putative active site residue, mutation severly impairs enzyme function
N224A
-
steady-state kinetic parameters are within an order of magnitude of the native enzyme
T131S
-
steady-state kinetic parameters are within an order of magnitude of the native enzyme
C260A
-
no oxidation of UDP-glucose to glucuronic acid, but capable of both reducing the aldehyde intermediate and oxidizing the hydrated form of the aldehyde intermediate, protein is expressed in inclusion bodies
E141Q
-
kcat-value 10fold lower than wild-type
E145Q
-
kcat-value 10fold lower than wild-type
T118A
-
160fold reduction of kcat value
additional information