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Ambler RP, Auffret AD, Clarke PH. The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa. FEBS Lett. 1987;215(2):285-90doi: 10.1016/0014-5793(87)80163-1.
Ambler, R. P., Auffret, A. D., & Clarke, P. H. (1987). The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa. FEBS letters, 215(2), 285-90. https://doi.org/10.1016/0014-5793(87)80163-1
Ambler, R P, et al. "The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa." FEBS letters vol. 215,2 (1987): 285-90. doi: https://doi.org/10.1016/0014-5793(87)80163-1
Ambler RP, Auffret AD, Clarke PH. The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa. FEBS Lett. 1987 May 11;215(2):285-90. doi: 10.1016/0014-5793(87)80163-1. PMID: 3108029.
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FEBS Lett. 1987 May 11;215(2):285-90. doi: 10.1016/0014-5793(87)80163-1.

The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa.

FEBS letters

R P Ambler, A D Auffret, P H Clarke

PMID: 3108029 DOI: 10.1016/0014-5793(87)80163-1
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Abstract

Amino acid sequence studies show that the aliphatic amidase (EC 3.5.1.4) from Pseudomonas aeruginosa PAC142 consists of a single polypeptide chain of 346 residues, giving an Mr of 38,400. The evidence from the amino acid studies is in complete agreement with that deduced from the DNA sequence of the amiE gene. Studies of the protein from Pseudomonas putida A87 show that it differs from the Ps. aeruginosa protein by about 30 amino acid substitutions. It now becomes possible to relate changes in the enzyme which result in altered specificity to structural changes in the protein.

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