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
4.3.1.1 aspartate ammonia-lyaseAdvanced search results
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Engineering on EC 4.3.1.1 - aspartate ammonia-lyase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
H188A
Bacillus sp. (in: Bacteria) YM55-1
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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
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S140G/T141G
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implicated in binding the C4 carboxylate group of substrate
S140K/T141K
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implicated in binding the C4 carboxylate group of substrate
K140I
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Km value 10fold higher than wild type, comparable increase in Ki for competitive inhibitors
K327N
mutant enzyme catalyzes the deamination of L-aspartic acid alpha-amide, 13.5fold increase in Km-value for L-aspartate compared to wild-type value
K55R
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completeley inactive and insoluble protein, reactivation by an artificial chaperone system including beta-cyclodextrin and cetyltrimethylammonium bromide
V363L
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mutation in primary structure causing dramatic differences in catalytic activity do not promote significant changes in secondary structure
additional information
additional information
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design of enzyme variants by ligation of subdomains with a random hexapeptide loop, variant with highest activity is a monomer with high thermotolerance
additional information
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mutant N217K/T233R/V367G through enzyme modification by direct evolution in order to enhance enzymic activity
additional information
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construction of hybrid enzyme from alpha-aspartyl dipeptidase and L-aspartase. The hybrid enzyme can be used in synthesis of the precursor for aspartame
additional information
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insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
additional information
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insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
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