mtgA:Quickview: Difference between revisions
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MtgA has flavomycin-resistant peptidoglycan synthesis activity (Di Berardino, 1996; Derouaux, 2007). mtgA is a non-essential gene (Schiffer, 1999). MtgA localizes to the division site and interacts with FtsW, FtsN, and FtsI in mcrA(Ts) mrcB- strains, indicating a role for MtgA in peptidoglycan synthesis related to the cell cycle (Derouaux, 2007). The use of the term transglycolase is ambiguous as it can describe both lytic and synthetic peptidoglycan activities, therefore glycosyltransferase is preferred (Di Berardino, 1996). MtgA lacks a penicillin binding domain and therefore is penicillin-insensitive. MtgA is a membrane-bound periplasmic enzyme that has an uncleaved signal anchor (Di Berardino, 1996). MtgA may be the glycan polymerase characterized by Hara (1984), although it has an apparent MW larger than MtgA (Di Berardino, 1996).<ref name='LIB:EcoGene'/> | MtgA has flavomycin-resistant peptidoglycan synthesis activity (Di Berardino, 1996 <ref name=PMID:8772200/>; Derouaux, 2007). mtgA is a non-essential gene (Schiffer, 1999). MtgA localizes to the division site and interacts with FtsW, FtsN, and FtsI in mcrA(Ts) mrcB- strains, indicating a role for MtgA in peptidoglycan synthesis related to the cell cycle (Derouaux, 2007). The use of the term transglycolase is ambiguous as it can describe both lytic and synthetic peptidoglycan activities, therefore glycosyltransferase is preferred (Di Berardino, 1996). MtgA lacks a penicillin binding domain and therefore is penicillin-insensitive. MtgA is a membrane-bound periplasmic enzyme that has an uncleaved signal anchor (Di Berardino, 1996). MtgA may be the glycan polymerase characterized by Hara (1984), although it has an apparent MW larger than MtgA (Di Berardino, 1996).<ref name='LIB:EcoGene'/> | ||
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==References== | ==References== | ||
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Revision as of 19:43, 7 October 2009
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
See Help:Quickview for help with entering information in the Quickview table.
| Standard Name |
mtgA |
|---|---|
| Gene Synonym(s) |
ECK3197, b3208, JW3175, yrbM, mgt[1] |
| Product Desc. |
biosynthetic peptidoglycan transglycosylase[2][3] Monofunctional peptidoglycan glycosyltransferase; monofunctional biosynthetic peptidoglycan transglycosylase; GTase; TGase[4] |
| Product Synonyms(s) |
biosynthetic peptidoglycan transglycosylase[1], B3208[2][1], Mgt[2][1], YrbM[2][1], MtgA[2][1] |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity |
|
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Notes
MtgA has flavomycin-resistant peptidoglycan synthesis activity (Di Berardino, 1996 [5]; Derouaux, 2007). mtgA is a non-essential gene (Schiffer, 1999). MtgA localizes to the division site and interacts with FtsW, FtsN, and FtsI in mcrA(Ts) mrcB- strains, indicating a role for MtgA in peptidoglycan synthesis related to the cell cycle (Derouaux, 2007). The use of the term transglycolase is ambiguous as it can describe both lytic and synthetic peptidoglycan activities, therefore glycosyltransferase is preferred (Di Berardino, 1996). MtgA lacks a penicillin binding domain and therefore is penicillin-insensitive. MtgA is a membrane-bound periplasmic enzyme that has an uncleaved signal anchor (Di Berardino, 1996). MtgA may be the glycan polymerase characterized by Hara (1984), although it has an apparent MW larger than MtgA (Di Berardino, 1996).[4]
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Di Berardino, M et al. (1996) The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes. FEBS Lett. 392 184-8 PubMed