A bacterial methyltransferase that initiates biotin synthesis, an attractive anti-ESKAPE druggable pathway.

PMID: 397053672024China

Key Findings

The study identifies and characterizes two BioC isoenzymes, AbBioC from Acinetobacter baumannii and KpBioC from Klebsiella pneumoniae, which function as malonyl-ACP methyltransferases in the initial step of biotin synthesis. These enzymes are crucial for biotin synthesis and play a role in colistin resistance in A. baumannii.

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2gene entries

18mutation entries

AMR Genes

Gene Name	Alleles	Encodes	Confers Resistance To	Organisms	Database	Validation Status
mcr-1	1	polymyxin resistance protein	Colistin	Acinetobacter baumannii Klebsiella pneumoniae	Reslit	-
mcr-4	1	polymyxin resistance protein	Colistin	Acinetobacter baumannii	Reslit	-

AMR Mutations

Gene	Protein Change	Nucleotide Change	Mechanism	Organism	Resistance To	Database	Validation Status
bioC	D75A	-	The D75A mutation disrupts SAM binding and reduces enzymatic activity, indicating a critical role in BioC function.	Klebsiella pneumoniae, Acinetobacter baumannii	Polymyxin	Reslit	-
bioC	Q116A	-	The Q116A mutation disrupts the neutralization of the malonyl group, affecting substrate binding and enzymatic activity.	Klebsiella pneumoniae, Acinetobacter baumannii	Polymyxin	Reslit	-
bioC	K194A	-	The K194A mutation affects the interaction with the ACP carrier, reducing enzymatic activity.

Browse Papers

A bacterial methyltransferase that initiates biotin synthesis, an attractive anti-ESKAPE druggable pathway.

AMR Genes

AMR Mutations