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Literature summary extracted from

  • Gross, M.; Hessefort, S.; Olin, A.
    Purification of a 38-kDa protein from rabbit reticulocyte lysate which promotes protein renaturation by heat shock protein 70 and its identification as delta-aminolevulinic acid dehydratase and as a putative DnaJ protein (1999), J. Biol. Chem., 274, 3125-3134.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.24 additional information Oryctolagus cuniculus the enzyme stimulates renaturation of luciferase by hsp 70 up to 10fold ?
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Organism

EC Number Organism UniProt Comment Textmining
4.2.1.24 Oryctolagus cuniculus
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Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.24
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Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.24 reticulocyte
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Oryctolagus cuniculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate
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Oryctolagus cuniculus porphobilinogen + 2 H2O
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?
4.2.1.24 additional information the enzyme stimulates renaturation of luciferase by hsp 70, a member of the heat shock protein 70kDa-family, up to 10fold Oryctolagus cuniculus ?
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?
4.2.1.24 additional information the enzyme stimulates renaturation of luciferase by hsp 70 up to 10fold Oryctolagus cuniculus ?
-
?