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Enzyme Nomenclature
Information on EC 3.1.1.103 - teichoic acid D-alanine hydrolase and Organism(s) Staphylococcus aureus and UniProt Accession O50608
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3.1.1.103 teichoic acid D-alanine hydrolaseIUBMB 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.
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Staphylococcus aureus
Reaction Schemes
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[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan
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[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fmtA
fmtA
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SYSTEMATIC NAME
IUBMB Comments
teichoic acid D-alanylhydrolase
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.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + H2O
[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + D-alanine
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-
-
?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala
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-
-
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?
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-alanine
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[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + H2O
[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + D-alanine
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additional information
?
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the enzyme hydrolyzes the ester bond between D-Ala and the backbone of teichoic acids, which are polyglycerol-phosphate or polyribitol-phosphate polymers found in the Staphylococcus aureus cell envelope
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?
additional information
?
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the enzyme shows very low esterase activity on 4-nitrophenyl butyrate and 4-nitrophenyl acetate, and no activity with D-alanine methyl ester and L-alanine 4-nitroanilide
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + H2O
[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + D-alanine
-
-
-
?
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + H2O
[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-ManNAc-GlcNAc-PP-peptidoglycan + D-alanine
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-
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?
additional information
?
-
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the enzyme hydrolyzes the ester bond between D-Ala and the backbone of teichoic acids, which are polyglycerol-phosphate or polyribitol-phosphate polymers found in the Staphylococcus aureus cell envelope
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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the enzyme is intrinsically resistant to beta-lactam inactivation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme mutants have increased susceptibilities to beta-lactams in the presence or absence of 0.02% Triton X-100 compared with the susceptibilities of the parent strains, while the susceptibilities of the mutants to other antibiotics are not altered
physiological function
malfunction
the inactivation of the enzyme in two methicillin-resistant Staphylococcus aureus strains does not cause a reduction in methicillin resistance
physiological function
physiological function
the enzyme affects the methicillin resistance level in methicillin-resistant Staphylococcus aureus
physiological function
the enzyme is involved in cell wall synthesis
physiological function
-
the enzyme has weak D-Ala-D-Ala-carboxypeptidase activity and is capable of covalently incorporating C14-Gly into cell walls
physiological function
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the enzyme is part of the core cell wall stimulon and is involved in methicillin resistance in Staphylococcus aureus
physiological function
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the enzyme modulates D-alanylation of teichoic acids and is involved in cell division, biofilm formation, autolysis, and colonization
physiological function
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the penicillin-binding protein may compensate for suppressed peptidoglycan biosynthesis underbeta-lactam induced cell wall stress conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S127A
S127A
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the mutant show strongly reduced activity and no DD-carboxypeptidase activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SP-Sepharose column chromatography, Hiprep butyl column chromatography, and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription of the enzyme is dose dependently increased by the addition of beta-lactam antibiotics, fosfomycin, and bacitracin
the transcription of the enzyme is not changed by the addition of vancomycin or tetracycline
SarA is essential for the induction of enzyme expression by cell wall-specific antibiotic
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Komatsuzawa, H.; Sugai, M.; Ohta, K.; Fujiwara, T.; Nakashima, S.; Suzuki, J.; Lee, C.; 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
2355-2361
1997
Staphylococcus aureus (O50608), Staphylococcus aureus KSA8 (O50608)
Komatsuzawa, H.; Ohta, K.; Labischinski, H.; Sugai, M.; Suginaka, H.
Characterization of fmtA, a gene that modulates the expression of methicillin resistance in Staphylococcus aureus
Antimicrob. Agents Chemother.
43
2121-2125
1999
Staphylococcus aureus (O50608), Staphylococcus aureus KSA8 (O50608)
Qamar, A.; Golemi-Kotra, D.
Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis
Antimicrob. Agents Chemother.
56
3797-3805
2012
Staphylococcus aureus, Staphylococcus aureus RN4220
Komatsuzawa, H.; Choi, G.; Fujiwara, T.; Huang, Y.; Ohta, K.; Sugai, M.; Suginaka, H.
Identification of a fmtA-like gene that has similarity to other PBPs and beta-lactamases in Staphylococcus aureus
FEMS Microbiol. Lett.
188
35-39
2000
Staphylococcus aureus (Q9KJ74), Staphylococcus aureus ISP3 (Q9KJ74)
Fan, X.; Liu, Y.; Smith, D.; Konermann, L.; Siu, K.; Golemi-Kotra, D.
Diversity of penicillin-binding proteins Resistance factor FmtA of Staphylococcus aureus
J. Biol. Chem.
282
35143-35152
2007
Staphylococcus aureus, Staphylococcus aureus Mu50
Rahman, M.; Hunter, H.; Prova, S.; Verma, V.; Qamar, A.; Golemi-Kotra, D.
The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids
mBio
7
e0207015
2016
Staphylococcus aureus
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