Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys70
Keyword(s):
Class D
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The activity of class D β-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D β-lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl–enzyme is the rate-limiting step for the wild-type OXA-10 β-lactamase.
2003 ◽
Vol 122
(3)
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pp. 295-306
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2020 ◽
1968 ◽
Vol 23
(4)
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pp. 547-554
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1977 ◽
Vol 2
(1)
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pp. 1-3
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Keyword(s):
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1972 ◽
Vol 20
(11)
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pp. 917-922
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2014 ◽
Vol 58
(8)
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pp. 4826-4836
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1999 ◽
Vol 12
(12)
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pp. 1082-1089
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2006 ◽
Vol 290
(2)
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pp. F313-F318
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