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- Title
Expression, Purification and Crystal Structure of a Truncated Acylpeptide Hydrolase from Aeropyrum pernix K1.
- Authors
Hai-Feng ZHANG; Bai-Song ZHENG; Ying PENG; Zhi-Yong LOU; Yan FENG; Zi-He RAO
- Abstract
Acylpeptide hydrolase (APH) catalyzes the N-terminal hydrolysis of Nα-acylpeptides to release Nα-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 Å using X-ray diffraction. A truncated mutant of apAPH that lacks the first short α-helix at the N-terminal, apAPH-α(1–21), was cloned, expressed, characterized and crystallized. Data from biochemical experiments indicate that the optimum temperature of apAPH is decreased by 15 °C with the deletion of the N-terminal α-helix. However, the enzyme activity at the optimal temperature does not change. It suggests that this N-terminal α-helix is essential for thermostability. Here, the crystal structure of apAPH-α(1–21) has been determined by molecular replacement to 2.5 å. A comparison between the two structures suggests a difference in thermostability, and it can be concluded that by adding or deleting a linking structure (located over different domains), the stability or even the activity of an enzyme can be modified.
- Subjects
HYDROLASES; ENZYMES; PEPTIDES; AMINO acids; THERMOPHILIC bacteria; THERMOPHILIC microorganisms; MOLECULAR structure
- Publication
Acta Biochimica et Biophysica Sinica, 2005, Vol 37, Issue 9, p613
- ISSN
1672-9145
- Publication type
Article
- DOI
10.1111/j.1745-7270.2005.00085.x