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Literature summary for 3.5.2.6 extracted from

  • Yamaguchi, Y.; Matsueda, S.; Matsunaga, K.; Takashio, N.; Toma-Fukai, S.; Yamagata, Y.; Shibata, N.; Wachino, J.; Shibayama, K.; Arakawa, Y.; Kurosaki, H.
    Crystal structure of IMP-2 metallo-beta-lactamase from Acinetobacter spp.: comparison of active-site loop structures between IMP-1 and IMP-2 (2015), Biol. Pharm. Bull., 38, 96-101.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene blaIMP-2, recombinant expression in Escherichia coli strain HB101 harboring pBC SK(+) Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme IMP-2 MBL, hanging drop vapour diffusion metod, mixxing of 0.003 ml of 5 mg/ml protein in 20 mM HEPES-NaOH, pH 7.5, with 0.003 ml of reservoir solution containing 30% w/v PEG 4000, 0.1 M citric acid/sodium citrate, and 0.2 M sodium acetate, pH 6.0, equilibration against 0.35 ml reservori solution, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, modeling and structure comparisons Acinetobacter baumannii

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a di-Zn(II)-containing hydrolase, coordination geometry of Zn2 in IMP-2 is different from that of IMP-1, unlike Zn1, the electron density map at Zn2 shows the existence of partially dissociated Zn(II) ion from the active site structure, overview Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
benzylpenicillin + H2O Acinetobacter baumannii the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring (2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
?
imipenem + H2O Acinetobacter baumannii the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring (5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii Q9KVZ2 gene blaIMP-2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme IMP-2 from Escherichia coli strain HB101 harboring pBC SK(+) by cation exchange chromatography, ultrafiltration and gel filtration, to over 95% purity Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzylpenicillin + H2O the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring Acinetobacter baumannii (2R,4S)-2-[(R)-carboxy(2-phenylacetamido)methyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid
-
?
imipenem + H2O the enzyme catalyzes the hydrolysis of the C-N bond of the beta-lactam ring Acinetobacter baumannii (5R)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-([2-[(iminomethyl)amino]ethyl]sulfanyl)-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
?

Synonyms

Synonyms Comment Organism
IMP-2
-
Acinetobacter baumannii
IMP-2 MBL
-
Acinetobacter baumannii
subclass B1 metallo-?-lactamase
-
Acinetobacter baumannii

General Information

General Information Comment Organism
evolution comparison of the structures of subclass B1 metallo-beta-lactamases IMP-1 and IMP-2, which have an 85% amino acid identity, suggests that the amino acid substitution at position 68 on a beta-strand (beta3) (Pro in IMP-1 versus Ser in IMP-2) may be a staple factor affecting the flexibility of loop 1 (comprising residues at positions 60-66, EVNGWGV). In the IMP-1 structure, loop 1 adopts an open, disordered conformation. Comparison of the active site structure between IMP-1 and IMP-2, loop 1 of IMP-2 forms a closed conformation in which the side chain of Trp64, involved in substrate binding, is oriented so as to cover the active site, even though there is an acetate ion in the active site of both IMP-1 and IMP-2. Loop 1 of IMP-2 has a more flexible structure in comparison to IMP-1 due to having a Ser residue instead of the Pro residue at position 68, indicating that this difference in sequence may be a trigger to induce a more flexible conformation in loop 1 Acinetobacter baumannii
physiological function the enzyme is involved in antibiotic resistance, catalyzing the hydrolysis of antibiotics such as benzylpenicillin and imipenem Acinetobacter baumannii