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Literature summary for 6.3.2.12 extracted from

  • Cheng, V.W.; Leung, K.S.; Kwok, J.S.; Leung, R.K.; Yang, K.Y.; Chan, R.C.; Kam, K.M.; Tsui, S.K.
    Phylogenetic and structural significance of dihydrofolate synthase (folC) mutations in drug-resistant Mycobacterium tuberculosis (2016), Microb. Drug Resist., 22, 545-551 .
    View publication on PubMed
Search for more literature for 6.3.2.12

Cloned(Commentary)

Cloned (Comment) Organism
gene folC, DNA and amino acid sequence determination and analysis, genetic structure and sequence comparisons, genotyping of 254 clinical isolates, phylogenetic analysis Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
A132E naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
A171A naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
A420V naturally occuring mutation in enzyme FolC in clinical isolates of both drug-resistant and drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
A457V naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
D111A naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
D135A naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
D324G naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
D384A naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
E153A naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
E153G naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
E40G naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
E40K naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
E434Q naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
F461F naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
G112S naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
G284G naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
G422G naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
I43A naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
I43F naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
I43S naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
I43T naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
I43V naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
additional information phylogenetic and structural significance of mutations in gene folC in drug-resistant Mycobacterium tuberculosis, overview. Genotyping of 254 clinical isolates. Enzyme residues E40, I43, S150, and E153 are the most frequently affected amino acid residues in resistant isolates with mutant enzymes, distribution of mutations in the genome-based phylogenetic tree, overview. Mutations at E40, I43, and S150 can alter the structure of the FolC putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket Mycobacterium tuberculosis
P21L naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
P356L naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
P8P naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
P9P naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
R268R naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
R410W naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
R49G naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis Mycobacterium tuberculosis
S150G naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
S335I naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis
V256A naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis I6Y0R5
-
-
Mycobacterium tuberculosis ATCC 25618 / H37Rv I6Y0R5
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-

Synonyms

Synonyms Comment Organism
FolC
-
 Mycobacterium tuberculosis
LH57_13380 gene name, UniProt Mycobacterium tuberculosis
Rv2447c
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
malfunction mutations at residues E40, I43, and S150 can alter the structure of FolC's putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket Mycobacterium tuberculosis
additional information homology modeling of wild-type and mutated FolC, docking study using hydroxydihydropteroate, the metabolic derivative of para-aminosalicylic acid (PAS), to evaluate the binding affinity changes. Para-aminosalicylic acid (PAS) is an example of an anti-tuberculosis agent that blocks the folate pathway in Mycobacterium tuberculosis Mycobacterium tuberculosis