Molecule Information

General Information of the Molecule (ID: Mol04281)

Name	Aminoglycoside O-phosphotransferase APH(3')-Ie ,Enterococcus faecalis
Synonyms	Aminoglycoside O-phosphotransferase APH(3')-Ie Click to Show/Hide
Molecule Type	Protein
*Click to Show/Hide the Complete Species Lineage*
Kingdom: Bacillati Phylum: Bacillota Class: Bacilli Order: Lactobacillales Family: Enterococcaceae Genus: Enterococcus Species: Enterococcus faecalis

Type(s) of Resistant Mechanism of This Molecule

ADTT: Aberration of the Drug's Therapeutic Target

Drug Resistance Data Categorized by Drug

Approved Drug(s)

1 drug(s) in total

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Ribostamycin

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Drug Resistance Data Categorized by Their Corresponding Mechanisms
Aberration of the Drug's Therapeutic Target (ADTT)		Click to Show/Hide
Disease Class: citrobacter gillenii infection [ICD-11: XN0FZ]			[1]
Resistant Disease	citrobacter gillenii infection [ICD-11: XN0FZ]		Disease Info
Resistant Drug	Ribostamycin		Drug Info
Molecule Alteration	Expression	Up-regulation
Experiment for Molecule Alteration	PCR
Experiment for Drug Resistance	Drug susceptibility testing
Mechanism Description	A novel aminoglycoside resistance gene, designated aph(3')-Ie, which confers resistance to ribostamycin, kanamycin, sisomicin and paromomycin, was identified in the chromosome of the animal bacterium Citrobacter gillenii DW61, which exhibited a multidrug resistance phenotype. APH(3')-Ie showed the highest amino acid identity of 74.90% with the functionally characterized enzyme APH(3')-Ia. Enzyme kinetics analysis demonstrated that it had phosphorylation activity toward four aminoglycoside substrates, exhibiting the highest affinity (K m, 4.22 ± 0.88 uM) and the highest catalytic efficiency [k cat/K m, (32.27 ± 8.14) x 104] for ribomycin. Similar to the other APH(3') proteins, APH(3')-Ie contained all the conserved functional sites of the APH family. The aph(3')-Ie homologous genes were present in C. gillenii isolates from different sources, including some of clinical significance.

References

Ref 1	APH(3')-Ie, an aminoglycoside-modifying enzyme discovered in a rabbit-derived Citrobacter gillenii isolate. Front Cell Infect Microbiol. 2024 Jul 30;14:1435123.