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MetaCyc Enzyme: penicillin-binding protein 1B

Gene: mrcB Accession Numbers: EG10605 (MetaCyc), b0149, ECK0148

Synonyms: pbpF, ponB, PBP1B, PBP1Bs

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of penicillin-binding protein 1B = [MrcB]2

Summary:
The murein sacculus (peptidoglycan) is a polymer made up of long chains of alternating N-acetylglucosamine and N-acetylmuramic acid residues crosslinked by peptide side chains. PBP1B is a bifunctional, inner membrane enzyme catalyzing the transglycosylation and transpeptidation of murein precursors in the formation of the murein sacculus.

There are three distinct proteins encoded by mrcB [Tamaki77]. These are α, β, and γ, and each has both transglycosylation and transpeptidation activities [Nakagawa82]. The major products α and γ are predicted to have a Mr of 94,100 and 88,800 respectively [BroomeSmith85]. The γ component is produced by initiation of translation at the second initiation codon for methionine at amino acid 46 of the α component [BroomeSmith85, Kato84]. The β component is the product of the removal of the amino-terminal 24 amino acids from the α component [Suzuki87]. The α form is required for growth when PBP1A and PBP3 are inhibited by antibiotics [Chalut01]. It has been shown that residues 2-7 and 11-13 are required for proper functioning of the α form, though the β and γ forms are active without these residues [Chalut01].

PBP1B has been found to be localized primarily to the inner membrane, but also to adhesion sites where the inner and outer membranes contact [Bayer90]. PBP1B is anchored in the inner membrane by a single hydrophobic segment from residues 64 to 87 [Edelman87]. PBP1B has an additional membrane association site due to hydrophobicity within the region of residues 88 to 250 [Wang96c]. When it is cleaved directly c-terminal to the transmembrane segment, the protein continues to associate with the membrane [Nicholas93].

PBP1B has been shown to exist as a homodimer which is more strongly associated with the peptidoglycan or the outer membrane than the monomer [Zijderveld91]. The dimer is able to bind penicillin G [Zijderveld91]. The part of the PBP1B protein necessary for formation of dimer lies in the amino-terminal portion that contains fewer than 405 amino acids [Zijderveld91]. PBP1B forms homodimers with respect to the form of the protein (α-α, β-β, or γ-γ) [Zijderveld91]. The cytoplasmic domain of PBP1B is not necessary for dimer formation [Chalut01]. Dimer formation does not involve disulfide bridges [Chalut99]. PBP1B is more active as a dimer than when it is measured in its monomeric state [Bertsche05]. PBP1B does not form a complex with PBP1A [Charpentier02]. PBP1B has been found to bind specifically to MipA and to form a trimeric complex with MipA and MltA (membrane-bound lytic transglycosylase), though PBP1B doesn't bind MltA alone [Vollmer99]. A number of in vitro and in vivo experiments revealed direct interactions between PBP1B and FtsN, PBP3, and AmiC and showed the presence of PBP3 is necessary for localization of PBP1B to the division septum [Bertsche06, Muller07a]. PBP1B also interacts with PBP1C [Schiffer99], Slt70, and MltB [vonRechenberg96]. PBP1B forms a complex with the outer membrane lipoprotein LpoB, and LpoB is essential for the in vivo function of PBP1B [Typas10, ParadisBleau10]. PBP1B fractionates with PBPs 1A, 2, 3, and 5 when separated through agarose, and with PBPs 1A-5 during chromatography through Sephacryl S-1000 [Leidenix89].

The transglycosylase domain of PBP1B is located upstream of the transpeptidase domain. It has been suggested that the protein is the product of a fusion between a transglycosylase gene and a downstream transpeptidase gene [Nakagawa84]. It has been shown that the region between the transmembrane segment and the transglycosylase domain has an effect on the activity of the protein. The conserved SXXK box at ser-510, the SXN box at ser-572, and the KTG box at lys-698 are necessary for transpeptidase and penicillin-binding activity [Lefevre97]. The junction between the transglycosylase and transpeptidase domains allows for some insertions of amino acids without affecting activity [Lefevre97]. The C-terminal portion of PBP1B beyond residue 780 is not necessary for activity [Kato85a]. Mutations of conserved amino acids within the five conserved motifs of the glycosyltransferase domain of PBP1B reveal the importance of these residues for enzyme activity [Terrak08].

Purified PBP1B is able to catalyze peptidoglycan chain elongation and crosslinkage due to its peptidoglycan transglycosylase and transpeptidase activities [Tamura80]. PBP1B prefers a disaccharide donor with a reactive group on C1 of MurNAc and an acceptor with polyprenyl pyrophosphate on C1 of MurNAc [Fraipont06]. PBP1B is capable of polymerizing tripeptide lipid II as well as pentapeptide lipid II [vanHeijenoort92]. FtsN stimulates the activities of PBP1B at low concentrations of PBP1B [Muller07a]. Penicillin-binding of PBP1B was highest at pH 4 [Amaral86]. Binding of antibiotics to PBP1B results in inhibition of transglycosylase or transpeptidase activities [Ohya78, Nozaki79, Matsubara80].

Mutants lacking PBP1B have a reduced murein surface density [Caparros94] and are hypersensitive to cephalosporins, penicillins [Suzuki78], and 5,6-cis carbapenems [Nozaki84]. Either PBP1B or PBP1A (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required for cell elongation because a PBP1B-PBP1A double mutation is generally lethal [Spratt75a, Suzuki78, Kato85a, Yousif85, Wientjes]. Inhibition of PBP1A and PBP1B with cefsulodin results in osmosensitive L-form-like cells that have 7% residual peptidoglycan content and can survive in rich hypertonic medium [JoseleauPetit07]. Inhibition of PBP1A and PBP1B does not affect incorporation of murein precursors into peptidoglycan during initiation of cell growth [delaRosa85], and lysis occurs only upon the onset of cell division [Garcia89]. Other studies suggest PBP1A and PBP1B act independently of the cell cycle [Wientjes]. Overproduction of inactive forms of PBP1B results in lysis of the cell due mainly to the action of lytic transglycosylases [Meisel03]. It is suggested that this may be due to the replacement within a murein synthesizing enzyme complex of an active transglycosylase-transpeptidase with an inactive one, resulting in the lytic hydrolases making cuts in the murein sacculus without replacement by the transglycosylase-transpeptidase [Meisel03]. A mutant lacking PBP1B is outcompeted by it parental strain in co-culture during stationary phase [Pepper06]. Inactivation of PBP2 or PBP3 in a mrcB- mutant results in immediate lysis [Garcia90, Garcia91]. Experiments have been performed involving inhibition or mutation of PBP1B alone or coupled with inhibition or mutation of other proteins involved in cell division and murein metabolism [Tamaki77, Schmidt81, Garcia90, Garcia91, Denome99, Chen03f].

The crystal structure of PBP1B in complex with its inhibitor, moenomycin, has been resolved at 2.16Å [Sung09].

PBP1B is required for survival in competitive growth assays; it is the only PBP that is essential under such conditions [Pepper06].

Review: [Holtje98]

Citations: [Spratt77a, Buchanan81, Vanderwel84, Ishino86, Asoh86, Kraus87, Satta88, Nakanishi88, Nozaki89, Den89, Subbotina89, denBlaauwen90, denBlaauwen90a, Sumita90, Pla90, Den90]

Locations: cell wall, inner membrane

Map Position: [164,730 -> 167,264]

Molecular Weight of Polypeptide: 94.292 kD (from nucleotide sequence), 91 kD (experimental) [Spratt75a ]

pI: 7.0 [Rojo84]

Unification Links: ASAP:ABE-0000516 , CGSC:483 , DIP:DIP-10252N , EchoBASE:EB0600 , EcoGene:EG10605 , EcoliWiki:b0149 , ModBase:P02919 , OU-Microarray:b0149 , PortEco:mrcB , PR:PRO_000023286 , Pride:P02919 , Protein Model Portal:P02919 , RefSeq:NP_414691 , RegulonDB:EG10605 , SMR:P02919 , String:511145.b0149 , UniProt:P02919

Relationship Links: CAZy:IN-FAMILY:GT51 , InterPro:IN-FAMILY:IPR001264 , InterPro:IN-FAMILY:IPR001460 , InterPro:IN-FAMILY:IPR011813 , InterPro:IN-FAMILY:IPR012338 , InterPro:IN-FAMILY:IPR023346 , InterPro:IN-FAMILY:IPR028166 , PDB:Structure:3FWL , PDB:Structure:3FWM , PDB:Structure:3VMA , Pfam:IN-FAMILY:PF00905 , Pfam:IN-FAMILY:PF00912 , Pfam:IN-FAMILY:PF14814

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred by computational analysis Inferred from experiment [Tamura80, Nakagawa84, Jha06, Ramachandran06, Chandrakala04, Schwartz01b, Terrak99, GOA01a]
GO:0008360 - regulation of cell shape Inferred from experiment Inferred by computational analysis [UniProtGOA11a, JoseleauPetit07, Schmidt81]
GO:0009252 - peptidoglycan biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, JoseleauPetit07]
GO:0046677 - response to antibiotic Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, JoseleauPetit07]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0071555 - cell wall organization Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Typas10, ParadisBleau10, Muller07a]
GO:0008144 - drug binding Inferred from experiment [Ohya78, Nozaki79, Komatsu80, Matsubara80, Masuyoshi81, Tsuchiya81, Shigi81, Ohya82, Rojo84a, Hashizume84, Rake84, Terrak99, Stembera02, Stembera02a]
GO:0008658 - penicillin binding Inferred from experiment Inferred by computational analysis [GOA01a, Terrak99]
GO:0008955 - peptidoglycan glycosyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Tamura80, Nakagawa84, Schwartz01b, Schwartz02, Chen03f, Chandrakala04, Fraipont06, Ramachandran06]
GO:0009002 - serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from experiment [Tamura80, Nakagawa84, Terrak99, Schwartz01b, Chandrakala04, Ramachandran06, Jha06]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0008233 - peptidase activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016757 - transferase activity, transferring glycosyl groups Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Bayer90]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Lasserre06]
GO:0071575 - integral component of external side of plasma membrane Inferred from experiment [Edelman87]
GO:0009274 - peptidoglycan-based cell wall Inferred by computational analysis [GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes cell division
cell processes protection drug resistance/sensitivity
cell structure murein
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)
metabolism central intermediary metabolism amino sugar conversions

Credits:
Created in EcoCyc 21-Mar-2006 by Shearer A , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: peptidoglycan glycosyltransferase (penicillin-binding protein 1B)

2 ditrans,octacis-undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl-L-alanyl-γ-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine[periplasmic space] <=> a peptidoglycan dimer (meso-diaminopimelate containing)[periplasmic space] + di-trans,octa-cis-undecaprenyl diphosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: peptidoglycan biosynthesis I (meso-diaminopimelate containing)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Activators (Allosteric): enduracidin [Tamura80]

Inhibitors (Unknown Mechanism): moenomycin [Tamura80] , vancomycin [Tamura80] , ristocetin [Tamura80] , tunicamycin [Ramachandran06] , nisin [Ramachandran06] , chlorobiphenyl vancomycin [Chen03f] , teicoplanin [Chen03f] , DCB-PV [Sinha01] , macarbomycin [Nakagawa84]


Enzymatic reaction of: peptidoglycan D,D-transpeptidase (penicillin-binding protein 1B)

2 a peptidoglycan dimer (meso-diaminopimelate containing)[periplasmic space] <=> a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)[periplasmic space] + D-alanine[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: peptidoglycan biosynthesis I (meso-diaminopimelate containing)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Inhibitors (Unknown Mechanism): cephaloridine [Tamura80] , DQ-2556 [Tanaka92a] , imipenem [Hashizume84] , compound 6 [Lee03d] , FK037 [Mine93] , cephalexin [Chandrakala04] , cephradine [Chandrakala04] , cefuroxime [Chandrakala04] , cephadroxil [Chandrakala04] , cefaclor [Chandrakala04] , ceftriaxone [Chandrakala04] , cefazolin [Chandrakala04] , cepharpirin [Chandrakala04] , meropenem [Chandrakala04] , aztreonam [Chandrakala04] , amoxicillin [Chandrakala04] , cefsulodin [delaRosa85] , ampicillin [delaRosa85, Chandrakala04] , moenomycin [Jha06, Ramachandran06] , vancomycin [Chandrakala04] , ristocetin [Chandrakala04] , penicillin G [Chandrakala04, Tamura80]


Sequence Features

Feature Class Location Citations Comment
Intrinsic-Sequence-Variant 1 -> 45
[UniProt10a]
Alternate sequence: missing; UniProt: (in isoform Gamma);
Transmembrane-Region 64 -> 87
[UniProt10]
UniProt: Helical; Signal-anchor for type II membrane protein;; Non-Experimental Qualifier: probably;
Protein-Segment 88 -> 250
[UniProt10]
UniProt: Membrane association; Sequence Annotation Type: region of interest;
Sequence-Conflict 103
[BroomeSmith85, Fujita94, UniProt10a]
Alternate sequence: A; UniProt: (in Ref. 1 and 2);
Protein-Segment 109 -> 200
[UniProt10]
UniProt: UvrB domain 2 homolog; Sequence Annotation Type: region of interest;
Protein-Segment 195 -> 367
[UniProt10]
UniProt: Transglycosylase; Sequence Annotation Type: region of interest;
Mutagenesis-Variant 233
[Terrak99, UniProt11]
Alternate sequence: Q; UniProt: Loss of wild-type glycan chain elongation activity. No complementation in strain defective in PBP-1b.
Active-Site 233
[UniProt10]
UniProt: Proton donor; for transglycosylase activity; Non-Experimental Qualifier: probably;
Mutagenesis-Variant 234
[Terrak99, UniProt11]
Alternate sequence: N; UniProt: 7-fold decrease in catalytic activity. No complementation in strain defective in PBP-1b.
Mutagenesis-Variant 290
[Terrak99, UniProt11]
Alternate sequence: Q; UniProt: 11-fold decrease in catalytic activity. Shows complementation activity in strain defective in PBP-1b.
Protein-Segment 444 -> 736
[UniProt10]
UniProt: Transpeptidase; Sequence Annotation Type: region of interest;
Active-Site 510
[Terrak99, UniProt11]
UniProt: Acyl-ester intermediate; for transpeptidase activity.
Sequence-Conflict 754
[Fujita94, UniProt10a]
Alternate sequence: PTP; UniProt: (in Ref. 2);

History:
10/20/97 Gene b0149 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10605; confirmed by SwissProt match.


References

Amaral86: Amaral L, Lee Y, Schwarz U, Lorian V (1986). "Penicillin-binding site on the Escherichia coli cell envelope." J Bacteriol 167(2);492-5. PMID: 3090016

Asoh86: Asoh S, Matsuzawa H, Ishino F, Strominger JL, Matsuhashi M, Ohta T (1986). "Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12." Eur J Biochem 160(2);231-8. PMID: 3533535

Bayer90: Bayer MH, Keck W, Bayer ME (1990). "Localization of penicillin-binding protein 1b in Escherichia coli: immunoelectron microscopy and immunotransfer studies." J Bacteriol 172(1);125-35. PMID: 2403537

Bertsche05: Bertsche U, Breukink E, Kast T, Vollmer W (2005). "In vitro murein peptidoglycan synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli." J Biol Chem 280(45);38096-101. PMID: 16154998

Bertsche06: Bertsche U, Kast T, Wolf B, Fraipont C, Aarsman ME, Kannenberg K, von Rechenberg M, Nguyen-Disteche M, den Blaauwen T, Holtje JV, Vollmer W (2006). "Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli." Mol Microbiol 61(3);675-90. PMID: 16803586

BroomeSmith85: Broome-Smith JK, Edelman A, Yousif S, Spratt BG (1985). "The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12." Eur J Biochem 147(2);437-46. PMID: 3882429

Buchanan81: Buchanan CE (1981). "Topographical distribution of penicillin-binding proteins in the Escherichia coli membrane." J Bacteriol 145(3);1293-8. PMID: 7009576

Caparros94: Caparros M, Quintela JC, de Pedro MA (1994). "Variability of peptidoglycan surface density in Escherichia coli." FEMS Microbiol Lett 121(1);71-6. PMID: 8082828

Chalut01: Chalut C, Charpentier X, Remy MH, Masson JM (2001). "Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein 1b after impairment of penicillin-binding proteins 1a and 3." J Bacteriol 183(1);200-6. PMID: 11114917

Chalut99: Chalut C, Remy MH, Masson JM (1999). "Disulfide bridges are not involved in penicillin-binding protein 1b dimerization in Escherichia coli." J Bacteriol 181(9);2970-2. PMID: 10217796

Chandrakala04: Chandrakala B, Shandil RK, Mehra U, Ravishankar S, Kaur P, Usha V, Joe B, deSousa SM (2004). "High-throughput screen for inhibitors of transglycosylase and/or transpeptidase activities of Escherichia coli penicillin binding protein 1b." Antimicrob Agents Chemother 48(1);30-40. PMID: 14693515

Charpentier02: Charpentier X, Chalut C, Remy MH, Masson JM (2002). "Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli." J Bacteriol 184(13);3749-52. PMID: 12057973

Chen03f: Chen L, Walker D, Sun B, Hu Y, Walker S, Kahne D (2003). "Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate." Proc Natl Acad Sci U S A 100(10);5658-63. PMID: 12714684

delaRosa85: de la Rosa EJ, de Pedro MA, Vazquez D (1985). "Penicillin binding proteins: role in initiation of murein synthesis in Escherichia coli." Proc Natl Acad Sci U S A 82(17);5632-5. PMID: 3898066

Den89: Den Blaauwen T, Wientjes FB, Kolk AH, Spratt BG, Nanninga N (1989). "Preparation and characterization of monoclonal antibodies against native membrane-bound penicillin-binding protein 1B of Escherichia coli." J Bacteriol 171(3);1394-401. PMID: 2466033

Den90: Den Blaauwen T, Pas E, Edelman A, Spratt BG, Nanninga N (1990). "Mapping of conformational epitopes of monoclonal antibodies against Escherichia coli penicillin-binding protein 1B (PBP 1B) by means of hybrid protein analysis: implications for the tertiary structure of PBP 1B." J Bacteriol 172(12);7284-8. PMID: 1701431

denBlaauwen90: den Blaauwen T, Nanninga N (1990). "Topology of penicillin-binding protein 1b of Escherichia coli and topography of four antigenic determinants studied by immunocolabeling electron microscopy." J Bacteriol 172(1);71-9. PMID: 1688425

denBlaauwen90a: den Blaauwen T, Aarsman M, Nanninga N (1990). "Interaction of monoclonal antibodies with the enzymatic domains of penicillin-binding protein 1b of Escherichia coli." J Bacteriol 172(1);63-70. PMID: 2403551

Denome99: Denome SA, Elf PK, Henderson TA, Nelson DE, Young KD (1999). "Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis." J Bacteriol 181(13);3981-93. PMID: 10383966

Edelman87: Edelman A, Bowler L, Broome-Smith JK, Spratt BG (1987). "Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli." Mol Microbiol 1(1);101-6. PMID: 3330753

Fraipont06: Fraipont C, Sapunaric F, Zervosen A, Auger G, Devreese B, Lioux T, Blanot D, Mengin-Lecreulx D, Herdewijn P, Van Beeumen J, Frere JM, Nguyen-Disteche M (2006). "Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate." Biochemistry 45(12);4007-13. PMID: 16548528

Fujita94: Fujita N, Mori H, Yura T, Ishihama A (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22(9);1637-9. PMID: 8202364

Garcia89: Garcia del Portillo F, de Pedro MA, Joseleau-Petit D, D'Ari R (1989). "Lytic response of Escherichia coli cells to inhibitors of penicillin-binding proteins 1a and 1b as a timed event related to cell division." J Bacteriol 171(8);4217-21. PMID: 2666392

Garcia90: Garcia del Portillo F, de Pedro MA (1990). "Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB." J Bacteriol 172(10);5863-70. PMID: 2211517

Garcia91: Garcia del Portillo F, de Pedro MA (1991). "Penicillin-binding protein 2 is essential for the integrity of growing cells of Escherichia coli ponB strains." J Bacteriol 173(14);4530-2. PMID: 2066344

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hashizume84: Hashizume T, Ishino F, Nakagawa J, Tamaki S, Matsuhashi M (1984). "Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa, and inhibition of enzyme activities due to the PBPs in E. coli." J Antibiot (Tokyo) 37(4);394-400. PMID: 6427167

Holtje98: Holtje JV (1998). "Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli." Microbiol Mol Biol Rev 62(1);181-203. PMID: 9529891

Ishino86: Ishino F, Park W, Tomioka S, Tamaki S, Takase I, Kunugita K, Matsuzawa H, Asoh S, Ohta T, Spratt BG (1986). "Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein." J Biol Chem 261(15);7024-31. PMID: 3009484

Jha06: Jha RK, de Sousa SM (2006). "Microplate assay for inhibitors of the transpeptidase activity of PBP1b of Escherichia coli." J Biomol Screen 11(8);1005-14. PMID: 17092918

JoseleauPetit07: Joseleau-Petit D, Liebart JC, Ayala JA, D'Ari R (2007). "Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesis." J Bacteriol 189(18);6512-20. PMID: 17586646

Kato84: Kato J, Suzuki H, Hirota Y (1984). "Overlapping of the coding regions for alpha and gamma components of penicillin-binding protein 1 b in Escherichia coli." Mol Gen Genet 196(3);449-57. PMID: 6094972

Kato85a: Kato J, Suzuki H, Hirota Y (1985). "Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli." Mol Gen Genet 200(2);272-7. PMID: 2993822

Komatsu80: Komatsu Y, Nishikawa T (1980). "Moxalactam (6059-S), a new 1-oxa-beta-lactam: binding affinity for penicillin-binding proteins of Escherichia coli K-12." Antimicrob Agents Chemother 17(3);316-21. PMID: 6448573

Kraus87: Kraus W, Holtje JV (1987). "Two distinct transpeptidation reactions during murein synthesis in Escherichia coli." J Bacteriol 169(7);3099-103. PMID: 3298212

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lee03d: Lee M, Hesek D, Suvorov M, Lee W, Vakulenko S, Mobashery S (2003). "A mechanism-based inhibitor targeting the DD-transpeptidase activity of bacterial penicillin-binding proteins." J Am Chem Soc 125(52);16322-6. PMID: 14692773

Lefevre97: Lefevre F, Remy MH, Masson JM (1997). "Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis." J Bacteriol 179(15);4761-7. PMID: 9244263

Leidenix89: Leidenix MJ, Jacoby GH, Henderson TA, Young KD (1989). "Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography." J Bacteriol 171(10);5680-6. PMID: 2676988

Masuyoshi81: Masuyoshi S, Inoue M, Takaoka M, Mitsuhashi S (1981). "Cefotaxime: binding affinity to penicillin-binding proteins and morphological changes of Escherichia coli and Pseudomonas aeruginosa." Arzneimittelforschung 31(7);1070-2. PMID: 6268122

Matsubara80: Matsubara N, Minami S, Matsuhashi M, Takaoka M, Mitsuhashi S (1980). "Affinity of cefoperazone for penicillin-binding proteins." Antimicrob Agents Chemother 18(1);195-9. PMID: 6448021

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