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Literature summary for 2.6.1.1 extracted from

  • Birolo, L.; Tutino, M.L.; Fontanella, B.; Gerday, C.; Mainolfi, K.; Pascarella, S.; Sannia, G.; Vinci, F.; Marino, G.
    Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling (2000), Eur. J. Biochem., 267, 2790-2802.
    View publication on PubMed
Search for more literature for 2.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
isolation of genomic DNA and construction of a genetic library, cloning of gene PhaspC, DNA and amino acid sequence determination, overexpression in Escherichia coli strain TY103 Pseudoalteromonas haloplanktis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information recombinant enzyme, high temperature dependence of Km Pseudoalteromonas haloplanktis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43776
-
 x * 43776, recombinant enzyme, DNA sequence determination and mass spectrometry Pseudoalteromonas haloplanktis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Pseudoalteromonas haloplanktis
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Pseudoalteromonas haloplanktis TAC 125
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas haloplanktis
-
-
-
Pseudoalteromonas haloplanktis TAC 125
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of native enzyme, purification of recombinant enzyme from Escherichia coli Pseudoalteromonas haloplanktis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Pseudoalteromonas haloplanktis
12.92
-
 recombinant enzyme in Escherichia coli cells Pseudoalteromonas haloplanktis
137.7
-
 purified recombinant enzyme Pseudoalteromonas haloplanktis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Pseudoalteromonas haloplanktis oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Pseudoalteromonas haloplanktis TAC 125 oxaloacetate + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
? x * 43776, recombinant enzyme, DNA sequence determination and mass spectrometry Pseudoalteromonas haloplanktis
More structure modeling, subunit organization Pseudoalteromonas haloplanktis

Synonyms

Synonyms Comment Organism
AspAT
-
 Pseudoalteromonas haloplanktis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Pseudoalteromonas haloplanktis
34
-
 optimal temperature of recombinant enzyme in Escherichia coli in vivo Pseudoalteromonas haloplanktis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 63 half-maximal activity at 35°C and 63°C Pseudoalteromonas haloplanktis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 t1/2: 6.8 min Pseudoalteromonas haloplanktis
50 65 recombinant enzyme, transition temperature Pseudoalteromonas haloplanktis
65.5
-
 recombinant enzyme, melting temperature Pseudoalteromonas haloplanktis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pseudoalteromonas haloplanktis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Pseudoalteromonas haloplanktis