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Literature summary for 4.2.1.24 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)

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Purification (Commentary)

Purification (Comment) Organism
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Oryctolagus cuniculus

Source Tissue

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-aminolevulinate + 5-aminolevulinate
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Oryctolagus cuniculus porphobilinogen + 2 H2O
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?
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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?
additional information the enzyme stimulates renaturation of luciferase by hsp 70 up to 10fold Oryctolagus cuniculus ?
-
?