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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1gt7

E.C. namerhamnulose-1-phosphate aldolase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 4.1.2.19
CSA Homologues of 1gt7There are 17 Homologs
CSA Entries With UniProtID P32169
CSA Entries With EC Number 4.1.2.19
PDBe Entry 1gt7
PDBSum Entry 1gt7
MACiE Entry 1gt7

Literature Report

IntroductionL-Rhamnulose-1-phosphate aldolase (RhuA) is a Class II aldolase, which infers the use of a divalent metal ion as an electron sink in the catalytic mechanism of the aldol cleavage and addition reactions. RhuA catalyses the cleavage of L-rhmnulose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. This enzyme also catalyses the reverse direction in making a carbon-carbon bond.
This enzyme shows similarities with L-fuculose-1-phosphate aldolase (FucA) and L-Ribulose-5-phosphate 4-epimerase (RibE).
MechansimThe reaction of L-Rhamnulose-1-phosphate is proposed as follows. The ring form of L-rhamnulose-1-phosphate is opened by the action of Glu 171 acting as a general acid/base catalyst, by protonation of the ring oxygen. The open form is stabilised by the zinc ion. A proton is abstracted from O4 of the diolate by the general base catalysis of Glu 117 to cause the split of the C3-C4 carbon bond and formation of a C3 carbanion - this is subsequently protonated by Glu 117 in general acid catalysis, and the products L-lactealdehyde and DHAP dissociate. The reaction can also proceed in the reverse direction.
Reaction

Catalytic Sites for 1gt7

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluA171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluB171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluC117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluC171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluD171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluE117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluE171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluF117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluF171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluG117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluG171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluH117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluH171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 9 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluI117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluI171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 10 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluJ117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluJ171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 11 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluK117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluK171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 12 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluL117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluL171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 13 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluM117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluM171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 14 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluN117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluN171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 15 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluO117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluO171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 16 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluP117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluP171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 17 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluQ117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluQ171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 18 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluR117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluR171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 19 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluS117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluS171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Annotated By Reference To The Literature - Site 20 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluT117117macie:sideChainActs as a general acid/base catalyst in splitting the C3-C4 bond.
GluT171171macie:sideChainActs as a general acid/base catalyst in opening of the ring form of L-rhamnulose-1-phosphate.

Literature References

Notes:
Kroemer M
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
Biochemistry 2003 42 10560-10568
PubMed: 12962479
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