(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Alphaproteobacteria: NE > Rhodospirillales: NE > Acetobacteraceae: NE > Acetobacter: NE > Acetobacter pasteurianus: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Acetobacter pasteurianus subsp. pasteurianus LMG 1262: N, E.
Acetobacter pasteurianus subsp. pasteurianus LMG 1262 = NBRC 106471: N, E.
Acetobacter pasteurianus IFO 3283-01-42C: N, E.
Acetobacter pasteurianus IFO 3283-07: N, E.
Acetobacter pasteurianus IFO 3283-12: N, E.
Acetobacter pasteurianus IFO 3283-22: N, E.
Acetobacter pasteurianus IFO 3283-03: N, E.
Acetobacter pasteurianus IFO 3283-32: N, E.
Acetobacter pasteurianus IFO 3283-26: N, E.
Acetobacter pasteurianus IFO 3283-01: N, E.
Acetobacter pasteurianus NBRC 101655: N, E.
Acetobacter pasteurianus 386B: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MVGQITLSKQKSVLQKKSLWASVALSGVLLAATLPVAQAAAPAADAAQAH DPLSVQTGSDIPASVHMPTDQQRDYIKREVMVPMRDGVKLYTVIVIPKNA RNAPILLTRTPYNAKGRANRVPNALTMREVLPQGDDVFVEGGYIRVFQDI RGKYGSQGDYVMTRPPHGPLNPTKTDETTDAWDTVDWLVHNVPESNGRVG MTGSSYEGFTVVMALLDPHPALKVAAPESPMVDGWMGDDWFHYGAFRQGA FDYFVSQMTARGGGNDIPRRDADDYTNFLKAGSAGSFATQAGLDQYPFWQ RMHAHPAYDAFWQGQALDKILAQRKPTVPMLWEQGLWDQEDMWGAIHAWQ ALKDADVKAPNTLVMGPWRHSGVNYNGSTLGPLEFEGDTAHQYRRDVFRP FFDEYLKPGSASVHLPDAIIYNTGDQKWDYYRSWPSVCESNCTGGLTPLY LADGHGLSFTHPAADGADSYVSDPAHPVPFISRPFAFAQSSRWKPWLVQD QREAESRPDVVTYETEVLDEPVRVSGVPVADLFAATSGTDSDWVVKLIDV QPAMTPDDPKMGGYELPVSMDIFRGRYRKDFAKPEALQPDATLHYHFTLP AVNHVFAKGHRIMVQIQSSWFPLYDRNPQKFVPNIFDAKPADYTVATQSI HHGGKEATSILLPVVKQ
The alpha-amino acid ester hydrolase (AEH) from Acetobacter turbidans is a bacterial enzyme catalyzing the hydrolysis and synthesis of beta-lactam antibiotics. The crystal structures of the native enzyme, both unliganded and in complex with the hydrolysis product D-phenylglycine are reported, as well as the structures of an inactive mutant (S205A) complexed with the substrate ampicillin, and an active site mutant (Y206A) with an increased tendency to catalyze antibiotic production rather than hydrolysis. The structure of the native enzyme shows an acyl binding pocket, in which D-phenylglycine binds, and an additional space that is large enough to accommodate the beta-lactam moiety of an antibiotic. In the S205A mutant, ampicillin binds in this pocket in a non-productive manner, making extensive contacts with the side chain of Tyr(112), which also participates in oxyanion hole formation. In the Y206A mutant, the Tyr(112) side chain has moved with its hydroxyl group toward the catalytic serine. Because this changes the properties of the beta-lactam binding site, this could explain the increased beta-lactam transferase activity of this mutant.
Title: Acetobacter turbidans alpha-amino acid ester hydrolase: merohedral twinning in P21 obscured by pseudo-translational NCS Barends TR, Dijkstra BW Ref: Acta Crystallographica D Biol Crystallogr, 59:2237, 2003 : PubMed
The structure elucidation of the alpha-amino acid ester hydrolase from Acetobacter turbidans by molecular replacement is described. In the monoclinic crystal, the molecules are related by both rotational and pseudo-crystallographic translational NCS (non-crystallographic symmetry). Refinement of the structure converged at unacceptably high R factors. After re-evaluation of the data, it was found that the crystal was merohedrally twinned, with a high twinning fraction. It is shown that the pseudo-crystallographic NCS causes aberrant behaviour of conventional twinning indicators, which explains why the twinning was only realized at the refinement stage.
Acetobacter pasteurianus (Acetobacter turbidans) alpha-amino acid ester hydrolase (EC 3.1.1.43)
