Literature DB >> 631987

The active site of an inducible arylacylamidase from Pseudomonas acidovorans.

E Heymann, H Rix.   

Abstract

Though very effectively ibhibited by both SH-group directed reagents and inhibitors typical for serine hydrolases, the inducible arylacylamidase from Pseudomonas acidovarans is a serine enzyme rather than a sulfhydryl enzyme. The amino acid sequence around the reactive serine residue is Gly-Ser-Ile. The sequence of a larger peptide from the active site is described.

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Year:  1978        PMID: 631987     DOI: 10.1111/j.1399-3011.1978.tb02821.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  1 in total

1.  N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant.

Authors:  Stephan Kolkenbrock; Katja Parschat; Bernd Beermann; Hans-Jürgen Hinz; Susanne Fetzner
Journal:  J Bacteriol       Date:  2006-10-13       Impact factor: 3.490

  1 in total

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