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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1brm

E.C. nameaspartate-semialdehyde dehydrogenase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 1.2.1.11
CSA Homologues of 1brmThere are 25 Homologs
CSA Entries With UniProtID P0A9Q9
CSA Entries With EC Number 1.2.1.11
PDBe Entry 1brm
PDBSum Entry 1brm
MACiE Entry 1brm

Literature Report

IntroductionAspartate-beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in the biosynthetic pathway that converts L-aspartic acid to lysine, isoleucine, methionine, threonine and metabolic intermediates such as diaminopimelic acid. The reaction catalysed is the reductive dephosphorylation of L-beta-aspartyl phosphate to L-aspartate-beta-semialdehyde, in the presence of NADPH. ASADH occurs in plants, most bacteria and fungi.
MechansimThe mechanism of ASADH is thought to be very similar to that of Glyceraldehyde-3-phosphate dehydrogenase [REF: 2]. In the suggested mechanism [REF: 3] the cysteine thiolate attacks the substrate carbonyl to form a thioester intermediate. This is followed by the transfer of a hydride to NADP to form NADPH. The oxygen anion of a bound inorganic phosphate attacks the thioester intermediate to expel the cysteine thiolate and to form the phosphorylated product.
Reaction

Catalytic Sites for 1brm

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
CysA135135macie:sideChain
HisA274274macie:sideChain
GlnA162162macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
CysB135135macie:sideChain
HisB274274macie:sideChain
GlnB162162macie:sideChain

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
CysC135135macie:sideChain
HisC274274macie:sideChain
GlnC162162macie:sideChain

Literature References

Notes:A similarity between the active sites of ASADH and Glyceraldehyde 3-phosphate dehydrogenase has been reported.
Karsten WE
Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli.
Biochim Biophys Acta 1992 1121 234-238
PubMed: 1350921
Hadfield A
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J Mol Biol 1999 289 991-1002
PubMed: 10369777
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