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270181 occurrences (No.97 in the rank) during 5 years in the PubMed. [cache]
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270181 occurrences (No.97 in the rank) during 5 years in the PubMed. [cache]
| 232) Pre-steady-state kinetic analysis indicates that the rate-limiting step for OXA-48 and OXA-163 hydrolysis of carbapenems is deacylation and that the greatly reduced carbapenemase activity of OXA-163 compared to that of OXA-48 is due entirely to a slower deacylation reaction. |
| PMID:33492952 DOI:10.1021/acsinfecdis.0c00798 |
| 2021 ACS infectious diseases |
| * Mechanistic Basis of OXA-48-like β-Lactamases' Hydrolysis of Carbapenems. |
| - Carbapenem-hydrolyzing class D β-lactamases (CHDLs) are an important source of resistance to these last resort β-lactam antibiotics. OXA-48 is a member of a group of CHDLs named OXA-48-like enzymes. On the basis of sequence similarity, OXA-163 can be classified as an OXA-48-like enzyme, but it has altered substrate specificity. Compared to OXA-48, it shows impaired activity for carbapenems but displays an enhanced hydrolysis of oxyimino-cephalosporins. Here, we address the mechanistic and structural basis for carbapenem hydrolysis by OXA-48-like enzymes. Pre-steady-state kinetic analysis indicates that the rate-limiting step for OXA-48 and OXA-163 hydrolysis of carbapenems is deacylation and that the greatly reduced carbapenemase activity of OXA-163 compared to that of OXA-48 is due entirely to a slower deacylation reaction. Furthermore, our structural data indicate that the positioning of the β5-β6 loop is necessary for carbapenem hydrolysis by OXA-48. A major difference between the OXA-48 and OXA-163 complexes with carbapenems is that the 214-RIEP-217 deletion in OXA-163 creates a large opening in the active site that is absent in the OXA-48/carbapenem structures. We propose that the larger active site results in less constraint on the conformation of the 6α-hydroxyethyl group in the acyl-enzyme. The acyl-enzyme intermediate assumes multiple conformations, most of which are incompatible with rapid deacylation. Consistent with this hypothesis, molecular dynamics simulations indicate that the most stable complex is formed between OXA-48 and imipenem, which correlates with the OXA-48 hydrolysis of imipenem being the fastest observed. Furthermore, the OXA-163 complexes with imipenem and meropenem are the least stable and show significant conformational fluctuations, which correlates with the slow hydrolysis of these substrates. |
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(40)2 measures |
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(15)5 placebo |
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(41)2 patients |
| (3)18 those |
(16)5 that |
(29)2 PLWH |
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| (4)16 healthy |
(17)4 standard |
(30)2 TM |
(43)2 poor |
| (5)13 a |
(18)4 women |
(31)2 TomTec |
(44)2 swabs |
| (6)13 controls |
(19)3 group |
(32)2 WT |
(45)2 therapy |
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(20)3 males |
(33)2 allogeneic |
(46)2 traditional |
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(21)3 no |
(34)2 any |
(47)2 uninfected |
| (9)7 their |
(22)3 non-obese |
(35)2 children |
(48)2 untreated |
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(23)3 wild-type |
(36)2 expert |
(49)2 usual |
| (11)6 individuals |
(24)2 B-385 |
(37)2 females |
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(25)2 CON |
(38)2 field |
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(26)2 CS- |
(39)2 irradiated |
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