The Enzyme Database

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EC 3.1.1.103     
Accepted name: teichoic acid D-alanine hydrolase
Reaction: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n D-alanine
Glossary: Rib-ol = ribitol
Other name(s): fmtA (gene name)
Systematic name: teichoic acid D-alanylhydrolase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C.Y. and Suginaka, H. Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 2355–2361. [PMID: 9371333]
2.  Qamar, A. and Golemi-Kotra, D. Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob. Agents Chemother. 56 (2012) 3797–3805. [DOI] [PMID: 22564846]
3.  Rahman, M.M., Hunter, H.N., Prova, S., Verma, V., Qamar, A. and Golemi-Kotra, D. The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids. MBio 7 (2016) e02070. [DOI] [PMID: 26861022]
[EC 3.1.1.103 created 2018]
 
 


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