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Literature summary extracted from

  • Ilic, S.; Cohen, S.; Singh, M.; Tam, B.; Dayan, A.; Akabayov, B.
    DnaG primase-A target for the development of novel antibacterial agents (2018), Antibiotics, 7, 72 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.7.101 drug development the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target Escherichia coli
2.7.7.101 drug development the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target Bacillus subtilis
2.7.7.101 drug development the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.101 (2E)-3-(6-chloro-2H-chromen-3-yl)acrylic acid
-
 Bacillus subtilis
2.7.7.101 (2E)-3-(6-chloro-2H-chromen-3-yl)acrylic acid
-
 Escherichia coli
2.7.7.101 (2E)-3-(6-chloro-2H-chromen-3-yl)acrylic acid
-
 Mycobacterium tuberculosis
2.7.7.101 2-((1H-indol-3-yl)thio)acetic acid
-
 Bacillus subtilis
2.7.7.101 2-((1H-indol-3-yl)thio)acetic acid
-
 Escherichia coli
2.7.7.101 2-((1H-indol-3-yl)thio)acetic acid
-
 Mycobacterium tuberculosis
2.7.7.101 2-fluoro-AraATP
-
 Bacillus subtilis
2.7.7.101 2-fluoro-AraATP
-
 Escherichia coli
2.7.7.101 2-fluoro-AraATP
-
 Mycobacterium tuberculosis
2.7.7.101 3-[2-(ethoxycarbonyl)-5-nitro-1H-indol-3-yl]propanoic acid
-
 Bacillus subtilis
2.7.7.101 3-[2-(ethoxycarbonyl)-5-nitro-1H-indol-3-yl]propanoic acid
-
 Escherichia coli
2.7.7.101 3-[2-(ethoxycarbonyl)-5-nitro-1H-indol-3-yl]propanoic acid
-
 Mycobacterium tuberculosis
2.7.7.101 4-fluorophenyl tetrazole
-
 Bacillus subtilis
2.7.7.101 4-fluorophenyl tetrazole
-
 Escherichia coli
2.7.7.101 4-fluorophenyl tetrazole
-
 Mycobacterium tuberculosis
2.7.7.101 7-nitro-1H-indole-2-carboxylic acid
-
 Bacillus subtilis
2.7.7.101 7-nitro-1H-indole-2-carboxylic acid
-
 Escherichia coli
2.7.7.101 7-nitro-1H-indole-2-carboxylic acid
-
 Mycobacterium tuberculosis
2.7.7.101 BAY 57-1293
-
 Bacillus subtilis
2.7.7.101 BAY 57-1293
-
 Escherichia coli
2.7.7.101 BAY 57-1293
-
 Mycobacterium tuberculosis
2.7.7.101 benzo[d]imidazo[2,1-b]imidazole lead structure for inhibitor search Bacillus subtilis
2.7.7.101 benzo[d]imidazo[2,1-b]imidazole lead structure for inhibitor search Escherichia coli
2.7.7.101 benzo[d]imidazo[2,1-b]imidazole lead structure for inhibitor search Mycobacterium tuberculosis
2.7.7.101 benzo[d]pyrimido[5,4-b]furan lead structure for inhibitor search Bacillus subtilis
2.7.7.101 benzo[d]pyrimido[5,4-b]furan lead structure for inhibitor search Escherichia coli
2.7.7.101 benzo[d]pyrimido[5,4-b]furan lead structure for inhibitor search Mycobacterium tuberculosis
2.7.7.101 cytosporone D
-
 Bacillus subtilis
2.7.7.101 cytosporone D
-
 Escherichia coli
2.7.7.101 cytosporone D
-
 Mycobacterium tuberculosis
2.7.7.101 doxorubicin contains aromatic structure with polar functional groups and is a potent (low-mM) DNA and nucleotide triphosphate competitive inhibitor, interacts with more than one site on Mycobacterium tuberculosis DnaG in order to block DNA and/or NTP binding Mycobacterium tuberculosis
2.7.7.101 geralcin C
-
 Bacillus subtilis
2.7.7.101 geralcin C
-
 Escherichia coli
2.7.7.101 geralcin C
-
 Mycobacterium tuberculosis
2.7.7.101 additional information inhibitor screening Bacillus subtilis
2.7.7.101 additional information inhibitor screening, three-dimensional pharmacophore development suggests inhibitors that contain two hydrophobes, two hydrogen bond acceptors, and a donor group Escherichia coli
2.7.7.101 additional information inhibitor screening Mycobacterium tuberculosis
2.7.7.101 pyrido[3',2'4,5]thieno[3,2-d]pyrimidine lead structure for inhibitor search Bacillus subtilis
2.7.7.101 pyrido[3',2'4,5]thieno[3,2-d]pyrimidine lead structure for inhibitor search Escherichia coli
2.7.7.101 pyrido[3',2'4,5]thieno[3,2-d]pyrimidine lead structure for inhibitor search Mycobacterium tuberculosis
2.7.7.101 sphingosine
-
 Bacillus subtilis
2.7.7.101 sphingosine
-
 Escherichia coli
2.7.7.101 sphingosine
-
 Mycobacterium tuberculosis
2.7.7.101 suramin contains aromatic structure with polar functional groups and is a potent (low-mM) DNA and nucleotide triphosphate competitive inhibitor, interacts with more than one site on Mycobacterium tuberculosis DnaG in order to block DNA and/or NTP binding Mycobacterium tuberculosis
2.7.7.101 vidarabine
-
 Bacillus subtilis
2.7.7.101 vidarabine
-
 Escherichia coli
2.7.7.101 vidarabine
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.101 ssDNA + n NTP Escherichia coli
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Bacillus subtilis
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Mycobacterium tuberculosis
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Bacillus subtilis 168
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Mycobacterium tuberculosis H37Rv
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP Mycobacterium tuberculosis ATCC 25618
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.101 Bacillus subtilis P05096
-
-
2.7.7.101 Bacillus subtilis 168 P05096
-
-
2.7.7.101 Escherichia coli P0ABS5
-
-
2.7.7.101 Mycobacterium tuberculosis P9WNW1
-
-
2.7.7.101 Mycobacterium tuberculosis ATCC 25618 P9WNW1
-
-
2.7.7.101 Mycobacterium tuberculosis H37Rv P9WNW1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.101 additional information Escherichia coli DnaG may utilize 2',3'-dideoxynucleoside 5'-triphosphates (ddNTPs) as substrates Escherichia coli ?
-
-
2.7.7.101 ssDNA + n NTP
-
 Escherichia coli ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Bacillus subtilis ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Mycobacterium tuberculosis ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Bacillus subtilis 168 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Mycobacterium tuberculosis H37Rv ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
2.7.7.101 ssDNA + n NTP
-
 Mycobacterium tuberculosis ATCC 25618 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.101 DnaG primase-A
-
 Escherichia coli
2.7.7.101 DnaG primase-A
-
 Bacillus subtilis
2.7.7.101 DnaG primase-A
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.7.101 evolution sequence and structural homology of DnaG-like primases, overview Escherichia coli
2.7.7.101 evolution sequence and structural homology of DnaG-like primases, overview Bacillus subtilis
2.7.7.101 evolution sequence and structural homology of DnaG-like primases, overview Mycobacterium tuberculosis
2.7.7.101 malfunction inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect Escherichia coli
2.7.7.101 malfunction inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect Bacillus subtilis
2.7.7.101 malfunction inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect Mycobacterium tuberculosis
2.7.7.101 additional information structure function relationship of DnaG primase, overview Escherichia coli
2.7.7.101 additional information structure function relationship of DnaG primase, overview Bacillus subtilis
2.7.7.101 additional information structure function relationship of DnaG primase, overview Mycobacterium tuberculosis
2.7.7.101 physiological function the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview Escherichia coli
2.7.7.101 physiological function the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview Bacillus subtilis
2.7.7.101 physiological function the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview Mycobacterium tuberculosis