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Overview for MACiE Entry M0228

Version history

General Information

EC Number: 4.2.1.46 (A member of the Lyases, Carbon-oxygen lyases, Hydro-lyases)

Enzyme Name: dTDP-glucose 4,6-dehydratase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P27830 - dTDP-glucose 4,6-dehydratase 2

Representative PDB Code: 1bxk - DTDP-GLUCOSE 4,6-DEHYDRATASE FROM E. COLI (Resolution = 1.90 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of dTDP-D-glucose

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Image of dTDP-4-dehydro-6-deoxy-alpha-D-glucose

Image of Water

dTDP-D-glucose
C00842
CHEBI:35248
dTDP-4-dehydro-6-deoxy-alpha-D-glucose
C11907
CHEBI:16128
Water
C00001
CHEBI:15377

This reaction is irreversible.


View similar reactions


Stepwise Description of the Reaction

Step 1Tyr160 deprotonates the 4-hydroxyl group of the substrate, which initiates the elimination of the substrate C4 hydride to the C4 position of NAD+.
Step 2Glu136 removes the C5 proton causing syn elimination of the 6-hydroxyl group, which is subsequently protonated by Asp135.
Step 3NADH eliminates a hydride from its C4 position to the C6 position of the intermediate, resulting in concomitant protonation of the C5 position with the proton donor being Glu136.
Step 4Asp135 deprotonates water, which in turn deprotonated Tyr160 in an inferred return step.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Tyr 160 A Side Chain
Lys 164 A Side Chain
Thr 134 A Side Chain
Asp 135 A Side Chain
Glu 136 A Side Chain

Organic Cofactors for M0228

Type Identity Chain
NAD NAD 380 A Overview

References

  1. A. D. Hegeman et al. (2002), Biochemistry, 41, 2797-2804. Concerted and stepwise dehydration mechanisms observed in wild-type and mutated Escherichia coli dTDP-glucose 4,6-dehydratase.
    Medline: 11851427
  2. B. Gerratana et al. (2001), Biochemistry, 40, 9187-9195. Mechanistic roles of Thr134, Tyr160, and Lys 164 in the reaction catalyzed by dTDP-glucose 4,6-dehydratase.
    Medline: 11478886
  3. S. T. M. Allard et al. (2001), J. Mol. Biol., 307, 283-295. The crystal structure of dTDP-D-Glucose 4,6-dehydratase (RmlB) from Salmonella enterica serovar Typhimurium, the second enzyme in the dTDP-l-rhamnose pathway.
    Medline: 11243820

Homologue information for M0228 (1bxk)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0255 alcohol dehydrogenase
1.1.1.1
1mg5 3.40.50.720
0.37140.3589Compare
M0092 UDP-glucose 6-dehydrogenase
1.1.1.22
1dli 3.40.50.720
0.71790.5304Compare
M0021 malate dehydrogenase (oxaloacetate-decarboxylating)
1.1.1.38
1do8 3.40.50.720
0.50.3856Compare
M0227 GDP-L-fucose synthase
1.1.1.271
1e6u 3.40.50.720
3.90.25.10
0.71420.2164Compare
M0110 D-amino-acid oxidase
1.4.3.3
1c0p 3.40.50.720
0.50580Compare
M0237 pteridine reductase
1.5.1.33
2c7v 3.40.50.720
0.69620.3319Compare
M0116 NAD(P)+ transhydrogenase (AB-specific)
1.6.1.2
1hzz 3.40.50.720
0.3870.3592Compare
M0142 ferredoxin-NADP+ reductase
1.18.1.2
1e6e 3.40.50.720
0.18180.2571Compare
M0090 adenosylhomocysteinase
3.3.1.1
1b3r 3.40.50.720
0.70.1927Compare
M0226 UDP-sulfoquinovose synthase
3.13.1.1
1qrr 3.40.50.720
3.90.25.10
0.8970.4231Compare
M0188 UDP-glucose 4-epimerase
5.1.3.2
1xel 3.40.50.720
3.90.25.10
0.57890.3549Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.40.50.720

View a comparison of the other reactions in MACiE with the CATH domain 3.90.25.10


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

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catalytic activity (molecular function)
binding (molecular function)
metabolic process (biological process)
dTDP-glucose 4,6-dehydratase activity (molecular function)
nucleotide-sugar metabolic process (biological process)
cellular metabolic process (biological process)
coenzyme binding (molecular function)
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