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Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1

, : Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1. Acta Biochimica et Biophysica Sinica 37(9): 613-617

Acylpeptide hydrolase (APH) catalyzes the N-terminal hydrolysis of N-alpha-acylpeptides to release N-alpha-acylated amino acids. The crystal structure of recombinant APH from the thermophilic archaeon Aeropyrum pernix K1 (apAPH) was reported recently to be at a resolution of 2.1 angstrom using X-ray diffraction. A truncated mutant of apAPH that lacks the first short a-helix at the N-terminal, apAPH-Delta(1-21), was cloned, expressed, characterized and crystallized.


PMID: 16143816

DOI: 10.1111/j.1745-7270.2005.00085.x

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