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Literature summary for 4.3.1.1 extracted from

  • Woods, S.A.; Miles, J.S.; Roberts, R.E.; Guest, J.R.
    Structural and functional relationships between fumarase and aspartase (1986), Biochem. J., 237, 547-557.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.3.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52190
-
 4 * 52190, calculation from sequence of amino acid Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K12
-
Serratia marcescens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate = fumarate + NH3 mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate r Escherichia coli fumarate + NH3
-
 ?
L-aspartate r Serratia marcescens fumarate + NH3
-
 ?
L-aspartate natural substrate Escherichia coli fumarate + NH3
-
 ?
L-aspartate natural substrate Serratia marcescens fumarate + NH3
-
 ?
additional information L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 52190, calculation from sequence of amino acid Escherichia coli