The Enzyme Database

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EC 3.5.1.133     
Accepted name: Nα-acyl-L-glutamine aminoacylase
Reaction: an Nα-acyl-L-glutamine + H2O = L-glutamine + a carboxylate
Other name(s): agaA (gene name); axillary malodor releasing enzyme; AMRE
Systematic name: Nα-acyl-L-glutamine amidohydrolase (carboxylate-forming)
Comments: Requires Zn2+. The enzyme, characterized from the bacterium Corynebacterium sp. Ax20, hydrolyses odorless Nα-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing axillary malodor compounds. While the enzyme is highly specific for the L-glutamine moiety, it is quite promiscuous regarding the acyl moiety. The two most common products of the enzyme’s activity in axillary secretions are (2E)-3-methylhex-2-enoate and 3-hydroxy-3-methylhexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Natsch, A., Gfeller, H., Gygax, P., Schmid, J. and Acuna, G. A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla. J. Biol. Chem. 278 (2003) 5718–5727. [PMID: 12468539]
2.  Natsch, A., Gfeller, H., Gygax, P. and Schmid, J. Isolation of a bacterial enzyme releasing axillary malodor and its use as a screening target for novel deodorant formulations. Int J Cosmet Sci 27 (2005) 115–122. [PMID: 18492161]
3.  Natsch, A., Derrer, S., Flachsmann, F. and Schmid, J. A broad diversity of volatile carboxylic acids, released by a bacterial aminoacylase from axilla secretions, as candidate molecules for the determination of human-body odor type. Chem. Biodivers. 3 (2006) 1–20. [PMID: 17193210]
[EC 3.5.1.133 created 2019]
 
 


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