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Literature summary for 4.1.2.13 extracted from

  • Choi, K.H.; Mazurkie, A.S.; Morris, A.J.; Utheza, D.; Tolan, D.R.; Allen, K.N.
    Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 Ang (1999), Biochemistry, 38, 12655-12664.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Oryctolagus cuniculus

Crystallization (Commentary)

Crystallization (Comment) Organism
complexed with fructose 1,6-bisphosphate Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
K146A is unable to cleave the C3-C4 bond of the hexose while retaining the ability to form the covalent intermediate, although at a greatly diminished rate Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate Oryctolagus cuniculus
-
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00883 rabbit
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Oryctolagus cuniculus glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Subunits

Subunits Comment Organism
tetramer
-
Oryctolagus cuniculus