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Identification of lysine at the active site of human 5-aminolaevulinate dehydratase.
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
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Cited by 9 PubMed Central articles
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X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase.
Erskine PT, Coates L, Butler D, Youell JH, Brindley AA, Wood SP, Warren MJ, Shoolingin-Jordan PM, Cooper JB.
Biochem J. 2003 Aug 1; 373(Pt 3):733-8.
[Biochem J. 2003]
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Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals.
Erskine PT, Senior N, Maignan S, Cooper J, Lambert R, Lewis G, Spencer P, Awan S, Warren M, Tickle IJ, et al.
Protein Sci. 1997 Aug; 6(8):1774-6.
[Protein Sci. 1997]
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Spatial proximity and sequence localization of the reactive sulfhydryls of porphobilinogen synthase.
Markham GD, Myers CB, Harris KA Jr, Volin M, Jaffe EK.
Protein Sci. 1993 Jan; 2(1):71-9.
[Protein Sci. 1993]
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