4.3.1.1: aspartate ammonia-lyase
This is an abbreviated version!
For detailed information about aspartate ammonia-lyase, go to the full flat file.
Reaction
Synonyms
ammonia-lyase, aspartate, ASPA, aspartase, aspartate ammonia lyase, aspartate ammonia-lyase, aspartate:ammonia lyase, aspB, Cj0087, fumaric aminase, L-aspartase, L-aspartate ammonia lyase, L-aspartate ammonia-lyase, maspase 1, maspase 2, maspase 3
ECTree
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Reaction
Reaction on EC 4.3.1.1 - aspartate ammonia-lyase
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mechanism
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L-aspartate = fumarate + NH3
the catalytic mechanism is studied by using a combined quantum-mechanical/molecular-mechanical (QM/MM) approach. Two elementary steps are calculated: The first step is the abstraction of Cbeta proton of L-aspartate by Ser318, which is calculated to be rate limiting. The second step is the cleavage of Calpha- N bond of L-aspartate to form fumarate and ammonia. Ser318 functions as the catalytic base, whereas His188 is a dispensable residue, but its protonation state can influence the active site structure
L-aspartate = fumarate + NH3
the catalytic mechanism is studied by using a combined quantum-mechanical/molecular-mechanical (QM/MM) approach. Two elementary steps are calculated: The first step is the abstraction of Cbeta proton of L-aspartate by Ser318, which is calculated to be rate limiting. The second step is the cleavage of Calpha- N bond of L-aspartate to form fumarate and ammonia. Ser318 functions as the catalytic base, whereas His188 is a dispensable residue, but its protonation state can influence the active site structure
Bacillus sp. (in: Bacteria) YM55-1
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