메뉴 건너뛰기




Volumn 5, Issue FEB, 2014, Pages

Characterization of serine hydroxymethyltransferase GlyA as a potential source of D-alanine in Chlamydia pneumoniae

Author keywords

Aberrant bodies; Alanine racemase; Chlamydial anomaly; D alanine; D cycloserine; GlyA; Penicillin; Persistence

Indexed keywords

ALANINE RACEMASE; CYCLOSERINE; DEXTRO ALANINE; GLYCINE HYDROXYMETHYLTRANSFERASE; PENICILLIN DERIVATIVE; ALANINE; RECOMBINANT PROTEIN;

EID: 84897925850     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2014.00019     Document Type: Article
Times cited : (25)

References (29)
  • 1
    • 0020313141 scopus 로고
    • Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid
    • Barbour, A. G., Amano, K., Hackstadt, T., Perry, L., and Caldwell, H. D. (1982). Chlamydia trachomatis has penicillin-binding proteins but not detectable muramic acid. J. Bacteriol. 151, 420-428.
    • (1982) J. Bacteriol. , vol.151 , pp. 420-428
    • Barbour, A.G.1    Amano, K.2    Hackstadt, T.3    Perry, L.4    Caldwell, H.D.5
  • 2
    • 0037586531 scopus 로고    scopus 로고
    • Genomic transcriptional profiling of the developmental cycle of Chlamydia trachomatis
    • doi: 10.1073/pnas.1331135100
    • Belland, R. J., Zhong, G., Crane, D. D., Hogan, D., Sturdevant, D., Sharma, J., et al. (2003). Genomic transcriptional profiling of the developmental cycle of Chlamydia trachomatis. Proc. Natl. Acad. Sci. U.S.A. 100, 8478-8483. doi: 10.1073/pnas.1331135100.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8478-8483
    • Belland, R.J.1    Zhong, G.2    Crane, D.D.3    Hogan, D.4    Sturdevant, D.5    Sharma, J.6
  • 3
    • 78650750259 scopus 로고    scopus 로고
    • Sexually transmitted diseases treatment guidelines
    • Centers for Disease Control and Prevention (CDC).
    • Centers for Disease Control and Prevention (CDC). (2010). Sexually transmitted diseases treatment guidelines. MMWR Recomm. Rep. 59, 1-110.
    • (2010) MMWR Recomm. Rep. , vol.59 , pp. 1-110
  • 4
    • 0035666383 scopus 로고    scopus 로고
    • L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions
    • doi: 10.1046/j.0014-2956.2001.02606.x
    • Contestabile, R., Paiardini, A., Pascarella, S., Di Salvo, M. L., D'aguanno, S., and Bossa, F. (2001). L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions. Eur. J. Biochem. 268, 6508-6525. doi: 10.1046/j.0014-2956.2001.02606.x.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6508-6525
    • Contestabile, R.1    Paiardini, A.2    Pascarella, S.3    Di Salvo, M.L.4    D'aguanno, S.5    Bossa, F.6
  • 5
    • 33751420220 scopus 로고    scopus 로고
    • Alanine racemase from the acidophile Acetobacter aceti
    • doi: 10.1016/j.pep.2006.05.016
    • Francois, J. A., and Kappock, T. J. (2007). Alanine racemase from the acidophile Acetobacter aceti. Protein Expr. Purif. 51, 39-48. doi: 10.1016/j.pep.2006.05.016.
    • (2007) Protein Expr. Purif. , vol.51 , pp. 39-48
    • Francois, J.A.1    Kappock, T.J.2
  • 6
    • 80053616695 scopus 로고    scopus 로고
    • Functional analysis of the cytoskeleton protein MreB from Chlamydophila pneumoniae
    • doi: 10.1371/journal.pone.0025129
    • Gaballah, A., Kloeckner, A., Otten, C., Sahl, H. G., and Henrichfreise, B. (2011). Functional analysis of the cytoskeleton protein MreB from Chlamydophila pneumoniae. PLoS ONE 6:e25129. doi: 10.1371/journal.pone.0025129.
    • (2011) PLoS ONE , vol.6
    • Gaballah, A.1    Kloeckner, A.2    Otten, C.3    Sahl, H.G.4    Henrichfreise, B.5
  • 7
    • 0032847094 scopus 로고    scopus 로고
    • Lack of cell wall peptidoglycan versus penicillin sensitivity: new insights into the chlamydial anomaly
    • Ghuysen, J. M., and Goffin, C. (1999). Lack of cell wall peptidoglycan versus penicillin sensitivity: new insights into the chlamydial anomaly. Antimicrob. Agents Chemother. 43, 2339-2344.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2339-2344
    • Ghuysen, J.M.1    Goffin, C.2
  • 8
    • 33746433456 scopus 로고    scopus 로고
    • Lateral transfers of serine hydroxymethyltransferase (glyA) and UDP-N-acetylglucosamine enolpyruvyl transferase (murA) genes from free-living Actinobacteria to the parasitic chlamydiae
    • doi: 10.1007/s00239-005-0286-x
    • Griffiths, E., and Gupta, R. S. (2006). Lateral transfers of serine hydroxymethyltransferase (glyA) and UDP-N-acetylglucosamine enolpyruvyl transferase (murA) genes from free-living Actinobacteria to the parasitic chlamydiae. J. Mol. Evol. 63, 283-296. doi: 10.1007/s00239-005-0286-x.
    • (2006) J. Mol. Evol. , vol.63 , pp. 283-296
    • Griffiths, E.1    Gupta, R.S.2
  • 10
    • 70350139038 scopus 로고    scopus 로고
    • Functional conservation of the lipid II biosynthesis pathway in the cell wall-less bacteria Chlamydia and Wolbachia: why is lipid II needed?
    • doi: 10.1371/journal.pone.0025129
    • Henrichfreise, B., Schiefer, A., Schneider, T., Nzukou, E., Poellinger, C., Hoffmann, T. J., et al. (2009). Functional conservation of the lipid II biosynthesis pathway in the cell wall-less bacteria Chlamydia and Wolbachia: why is lipid II needed? Mol. Microbiol. 73, 913-923. doi: 10.1371/journal.pone.0025129.
    • (2009) Mol. Microbiol. , vol.73 , pp. 913-923
    • Henrichfreise, B.1    Schiefer, A.2    Schneider, T.3    Nzukou, E.4    Poellinger, C.5    Hoffmann, T.J.6
  • 11
    • 79951603649 scopus 로고    scopus 로고
    • Upregulation of MetC is essential for D-alanine-independent growth of an alr/dadX-deficient Escherichia coli strain
    • doi: 10.1128/JB.01027-10
    • Kang, L., Shaw, A. C., Xu, D., Xia, W., Zhang, J., Deng, J., et al. (2011). Upregulation of MetC is essential for D-alanine-independent growth of an alr/dadX-deficient Escherichia coli strain. J. Bacteriol. 193, 1098-1106. doi: 10.1128/JB.01027-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 1098-1106
    • Kang, L.1    Shaw, A.C.2    Xu, D.3    Xia, W.4    Zhang, J.5    Deng, J.6
  • 12
    • 0015351329 scopus 로고
    • Mechanism of D-cycloserine action: alanine racemase from Escherichia coli
    • Lambert, M. P., and Neuhaus, F. C. (1972). Mechanism of D-cycloserine action: alanine racemase from Escherichia coli. W. J. Bacteriol. 110, 978-987.
    • (1972) W. J. Bacteriol. , vol.110 , pp. 978-987
    • Lambert, M.P.1    Neuhaus, F.C.2
  • 13
    • 84896708374 scopus 로고    scopus 로고
    • A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis
    • doi: 10.1038/nature12892. [Epub ahead of print].
    • Liechti, G. W., Kuru, E., Hall, E., Kalinda, A., Brun, Y. V., Vannieuwenhze, M., et al. (2013). A new metabolic cell-wall labelling method reveals peptidoglycan in Chlamydia trachomatis. Nature. doi: 10.1038/nature12892. [Epub ahead of print].
    • (2013) Nature
    • Liechti, G.W.1    Kuru, E.2    Hall, E.3    Kalinda, A.4    Brun, Y.V.5    Vannieuwenhze, M.6
  • 14
    • 33845221534 scopus 로고    scopus 로고
    • L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine
    • doi: 10.1073/pnas.0608643103
    • McCoy, A. J., Adams, N. E., Hudson, A. O., Gilvarg, C., Leustek, T., and Maurelli, A. T. (2006). L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. Proc. Natl. Acad. Sci. U.S.A. 103, 17909-17914. doi: 10.1073/pnas.0608643103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17909-17914
    • McCoy, A.J.1    Adams, N.E.2    Hudson, A.O.3    Gilvarg, C.4    Leustek, T.5    Maurelli, A.T.6
  • 15
    • 21244447071 scopus 로고    scopus 로고
    • Characterization of Chlamydia MurC-Ddl, a fusion protein exhibiting D-alanyl-D-alanine ligase activity involved in peptidoglycan synthesis and D-cycloserine sensitivity
    • doi: 10.1111/j.1365-2958.2005.04661.x
    • McCoy, A. J., and Maurelli, A. T. (2005). Characterization of Chlamydia MurC-Ddl, a fusion protein exhibiting D-alanyl-D-alanine ligase activity involved in peptidoglycan synthesis and D-cycloserine sensitivity. Mol. Microbiol. 57, 41-52. doi: 10.1111/j.1365-2958.2005.04661.x.
    • (2005) Mol. Microbiol. , vol.57 , pp. 41-52
    • McCoy, A.J.1    Maurelli, A.T.2
  • 16
    • 31944450440 scopus 로고    scopus 로고
    • Building the invisible wall: updating the chlamydial peptidoglycan anomaly
    • doi: 10.1016/j.tim.2005.12.004
    • McCoy, A. J., and Maurelli, A. T. (2006). Building the invisible wall: updating the chlamydial peptidoglycan anomaly. Trends Microbiol. 14, 70-77. doi: 10.1016/j.tim.2005.12.004.
    • (2006) Trends Microbiol. , vol.14 , pp. 70-77
    • McCoy, A.J.1    Maurelli, A.T.2
  • 17
    • 0017037598 scopus 로고
    • Steady state and exchange kinetics of pyruvate, phosphate dikinase from Propionibacterium shermanii
    • Milner, Y., and Wood, H. G. (1976). Steady state and exchange kinetics of pyruvate, phosphate dikinase from Propionibacterium shermanii. J. Biol. Chem. 251, 7920-7928.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7920-7928
    • Milner, Y.1    Wood, H.G.2
  • 18
    • 1942426774 scopus 로고
    • Inhibition of the growth of agents of the psittacosis group by d-cycloserine and its specific reversal by d-alanine
    • Moulder, J. W., Novosel, D. L., and Officer, J. E. (1963). Inhibition of the growth of agents of the psittacosis group by d-cycloserine and its specific reversal by d-alanine. J. Bacteriol. 85, 707-711.
    • (1963) J. Bacteriol. , vol.85 , pp. 707-711
    • Moulder, J.W.1    Novosel, D.L.2    Officer, J.E.3
  • 19
    • 84862755531 scopus 로고    scopus 로고
    • Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division
    • doi: 10.1111/j.1365-2958.2012.08100.x
    • Ouellette, S. P., Karimova, G., Subtil, A., and Ladant, D. (2012). Chlamydia co-opts the rod shape-determining proteins MreB and Pbp2 for cell division. Mol. Microbiol. 85, 164-178. doi: 10.1111/j.1365-2958.2012.08100.x.
    • (2012) Mol. Microbiol. , vol.85 , pp. 164-178
    • Ouellette, S.P.1    Karimova, G.2    Subtil, A.3    Ladant, D.4
  • 20
    • 72449141640 scopus 로고    scopus 로고
    • Functional and biochemical analysis of the Chlamydia trachomatis ligase MurE
    • doi: 10.1128/JB.01029-09
    • Patin, D., Bostock, J., Blanot, D., Mengin-Lecreulx, D., and Chopra, I. (2009). Functional and biochemical analysis of the Chlamydia trachomatis ligase MurE. J. Bacteriol. 191, 7430-7435. doi: 10.1128/JB.01029-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 7430-7435
    • Patin, D.1    Bostock, J.2    Blanot, D.3    Mengin-Lecreulx, D.4    Chopra, I.5
  • 21
    • 84865862961 scopus 로고    scopus 로고
    • Biochemical characterisation of the chlamydial MurF ligase, and possible sequence of the chlamydial peptidoglycan pentapeptide stem
    • doi: 10.1007/s00203-011-0784-8
    • Patin, D., Bostock, J., Chopra, I., Mengin-Lecreulx, D., and Blanot, D. (2012). Biochemical characterisation of the chlamydial MurF ligase, and possible sequence of the chlamydial peptidoglycan pentapeptide stem. Arch. Microbiol. 194, 505-512. doi: 10.1007/s00203-011-0784-8.
    • (2012) Arch. Microbiol. , vol.194 , pp. 505-512
    • Patin, D.1    Bostock, J.2    Chopra, I.3    Mengin-Lecreulx, D.4    Blanot, D.5
  • 22
    • 84868148846 scopus 로고    scopus 로고
    • Chlamydia muridarum enters a viable but non-infectious state in amoxicillin-treated BALB/c mice
    • doi: 10.1016/j.micinf.2012.07.017
    • Phillips Campbell, R., Kintner, J., Whittimore, J., and Schoborg, R. V. (2012). Chlamydia muridarum enters a viable but non-infectious state in amoxicillin-treated BALB/c mice. Microbes Infect. 14, 1177-1185. doi: 10.1016/j.micinf.2012.07.017.
    • (2012) Microbes Infect. , vol.14 , pp. 1177-1185
    • Phillips Campbell, R.1    Kintner, J.2    Whittimore, J.3    Schoborg, R.V.4
  • 23
    • 84890205605 scopus 로고    scopus 로고
    • Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ
    • doi: 10.1038/ncomms3856
    • Pilhofer, M., Aistleitner, K., Biboy, J., Gray, J., Kuru, E., Hall, E., et al. (2013). Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ. Nat. Commun. 4:2856. doi: 10.1038/ncomms3856.
    • (2013) Nat. Commun. , vol.4 , pp. 2856
    • Pilhofer, M.1    Aistleitner, K.2    Biboy, J.3    Gray, J.4    Kuru, E.5    Hall, E.6
  • 24
    • 0024291314 scopus 로고
    • Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D-and L-alanine
    • doi: 10.1021/bi00421a006
    • Shostak, K., and Schirch, V. (1988). Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D-and L-alanine. Biochemistry 27, 8007-8014. doi: 10.1021/bi00421a006.
    • (1988) Biochemistry , vol.27 , pp. 8007-8014
    • Shostak, K.1    Schirch, V.2
  • 25
    • 70450208343 scopus 로고    scopus 로고
    • Penicillin induced persistence in Chlamydia trachomatis: high quality time lapse video analysis of the developmental cycle
    • doi: 10.1371/journal.pone.0007723
    • Skilton, R. J., Cutcliffen, L. T., Barlow, D., Wang, Y., Salim, O., Lambden, P. R., et al. (2009). Penicillin induced persistence in Chlamydia trachomatis: high quality time lapse video analysis of the developmental cycle. PLoS ONE 4:e7723. doi: 10.1371/journal.pone.0007723.
    • (2009) PLoS ONE , vol.4
    • Skilton, R.J.1    Cutcliffen, L.T.2    Barlow, D.3    Wang, Y.4    Salim, O.5    Lambden, P.R.6
  • 26
    • 0032561496 scopus 로고    scopus 로고
    • Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis
    • doi: 10.1126/science.282.5389.754
    • Stephens, R. S., Kalman, S., Lammel, C., Fan, J., Marathe, R., Aravind, L., et al. (1998). Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis. Science 282, 754-759. doi: 10.1126/science.282.5389.754.
    • (1998) Science , vol.282 , pp. 754-759
    • Stephens, R.S.1    Kalman, S.2    Lammel, C.3    Fan, J.4    Marathe, R.5    Aravind, L.6
  • 27
    • 0000837032 scopus 로고
    • Competitive inhibition of enzymatic reactions by oxamycin
    • doi: 10.1021/ja01489a058
    • Strominger, J. L., Ito, E., and Threnn, R. H. (1960). Competitive inhibition of enzymatic reactions by oxamycin. J. Am. Chem. Soc. 82, 998-999. doi: 10.1021/ja01489a058.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 998-999
    • Strominger, J.L.1    Ito, E.2    Threnn, R.H.3
  • 28
    • 84875938556 scopus 로고    scopus 로고
    • Requirement of lipid II biosynthesis for cell division in cell wall-less Wolbachia, endobacteria of arthropods and filarial nematodes
    • doi: 10.1016/j.ijmm.2013.01.002
    • Vollmer, J., Schiefer, A., Schneider, T., Jülicher, K., Johnston, K. L., Taylor, M. J., et al. (2013). Requirement of lipid II biosynthesis for cell division in cell wall-less Wolbachia, endobacteria of arthropods and filarial nematodes. Int. J. Med. Microbiol. 303, 140-149. doi: 10.1016/j.ijmm.2013.01.002.
    • (2013) Int. J. Med. Microbiol. , vol.303 , pp. 140-149
    • Vollmer, J.1    Schiefer, A.2    Schneider, T.3    Jülicher, K.4    Johnston, K.L.5    Taylor, M.J.6
  • 29
    • 3543117812 scopus 로고    scopus 로고
    • Pre-exposure of infected human endometrial epithelial cells to penicillin in vitro renders Chlamydia trachomatis refractory to azithromycin
    • doi: 10.1093/jac/dkh283
    • Wyrick, P. B., and Knight, S. T. (2004). Pre-exposure of infected human endometrial epithelial cells to penicillin in vitro renders Chlamydia trachomatis refractory to azithromycin. J. Antimicrob. Chemother. 54, 79-85. doi: 10.1093/jac/dkh283.
    • (2004) J. Antimicrob. Chemother. , vol.54 , pp. 79-85
    • Wyrick, P.B.1    Knight, S.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.