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Volumn 7, Issue C, 1972, Pages 213-258

Aldolases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956895467     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6047(08)60450-3     Document Type: Article
Times cited : (314)

References (232)
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    • have recently obtained evidence which suggests that the active site lysine residue in oxalacetate decarboxylase has an abnormally low pK, which would favor Schiff base formation at neutral pH. In the case of fructose-1,6-diphosphate aldolase, the presence of the negatively charged phosphate group would form subsequent protonation of the Schiff base nitrogen atom.
    • Schmidt, D.E. Jr., Westheimer, F.H., Biochemistry, 10, 1971, 1249 have recently obtained evidence which suggests that the active site lysine residue in oxalacetate decarboxylase has an abnormally low pK, which would favor Schiff base formation at neutral pH. In the case of fructose-1,6-diphosphate aldolase, the presence of the negatively charged phosphate group would form subsequent protonation of the Schiff base nitrogen atom.
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