Identification of lysine at the active site of hum...[Biochem J. 1986]

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1: Biochem J. 1986 Jun 1;236(2):447-51. Links

Identification of lysine at the active site of human 5-aminolaevulinate dehydratase.

Gibbs PN, Jordan PM.

Reduction of human 5-aminolaevulinate dehydratase with NaBH4 in the presence of 14C-labelled substrate led to complete loss of catalytic activity and to incorporation of label into the enzyme protein. By comparison with authentic lysyl-aminolaevulinic acid, prepared chemically, the modified active-site amino acid obtained by acid hydrolysis was shown to be lysine. Sequencing of a CNBr-cleavage peptide isolated from the inactivated 14C-labelled enzyme revealed that the lysine was present within the sequence M-V-K-P-G-M.

PMID: 3092810 [PubMed - indexed for MEDLINE]

PMCID: PMC1146860

Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli. [Biochem J. 1995]
Lysine as the substrate binding site of porphobilinogen synthase of Rhodopseudomonas spheroides. [Z Naturforsch [C]. 1978]
Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit. [J Biol Chem. 1988]
Mechanism of action of 5-aminolaevulinate dehydratase from human erythrocytes. [Biochem J. 1985]
Characterization of a recombinant pea 5-aminolevulinic acid dehydratase and comparative inhibition studies with the Escherichia coli dehydratase. [Biochemistry. 1997]
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Identification of lysine at the active site of human 5-aminolaevulinate dehydratase.

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