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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1dli

E.C. nameUDP-glucose 6-dehydrogenase
SpeciesStreptococcus pyogenes (Bacteria)
E.C. Number (IntEnz) 1.1.1.22
CSA Homologues of 1dliThere are 11 Homologs
CSA Entries With UniProtID P0C0F4
CSA Entries With EC Number 1.1.1.22
PDBe Entry 1dli
PDBSum Entry 1dli
MACiE Entry M0092

Literature Report

IntroductionBacterial UDP-glucose dehydrogenase is essential for the formation of the antiphagocytic capsule that protects many virulent bacteria from the host's immune system. The homodimeric enzyme is composed of an N-terminal NAD+ dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long central alpha helix.
The enzyme catalyses the NAD+ dependent oxidation of UDP-glucose to UDP-glucuronic acid. In mammals this is the substrate for UDP-glucuronosyl transferases in the liver. UDP-glucuronosyl transferases catalyse the formation of glucuronide conjugates with various substances e.g. bilirubin - aiding its excretion.
MechansimThe active site contains residues contributed from the N- and C-terminal domains as well as from the central alpha-helix. THR 118 from the N-terminal forms a hydrogen bond to an ordered active site water molecule, that may be critical for the catalytic mechanism. SER 117 and PRO 120 are also probably essential for proper orientation of the catalytic THR 118. The central alpha-helix contributes two active site residues; LYS 204 and ASN 208. GLU 141 forms a hydrogen bond to the key catalytic residue LYS 204. The C-terminal contributes two residues; CYS 260 and ASP 264, both having direct roles in the enzyme mechanism.
Two complex mechanisms exist utilising the residues named above have been proposed [1].
Reaction

Catalytic Sites for 1dli

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA264264macie:sideChain
LysA204204macie:sideChain
ThrA118118macie:sideChain
AsnA208208macie:sideChain
GluA145145macie:sideChain
CysA260260macie:sideChain

Literature References

Notes:
Campbell RE
The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation.
Biochemistry 2000 39 7012-7023
PubMed: 10841783
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