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Literature summary for 4.3.1.1 extracted from

  • Zhang, J.; Liu, Y.
    A QM/MM study of the catalytic mechanism of aspartate ammonia lyase (2014), J. Mol. Graph. Model., 51, 113-119.
    View publication on PubMed
Search for more literature for 4.3.1.1

Protein Variants

Protein Variants Comment Organism
H188A mutation of His188 to Ala only changes the active site structure and slightly elongates the distance of Cbeta proton of substrate with Ser318, causing the enzyme to remain significant but reduced activity Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria) Q9LCC6
-
-
Bacillus sp. (in: Bacteria) YM55-1 Q9LCC6
-
-

Reaction

Reaction Comment Organism Reaction ID
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)
a

Synonyms

Synonyms Comment Organism
aspB
-
 Bacillus sp. (in: Bacteria)
L-aspartate ammonia-lyase
-
 Bacillus sp. (in: Bacteria)