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Literature summary for 2.3.1.180 extracted from
- Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents (2013), ChemMedChem, 8, 1589-1608.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate | - |
Escherichia coli |  |
| 1-(4-[(E)-[3-(benzyloxy)benzylidene]amino]phenyl)-3-phenylthiourea | molecular docking indicates that the compound has one hydrogen bonding interaction with Thr 81 of Escherichia coli FabH | Escherichia coli | |
| 1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea | - |
Escherichia coli | |
| 1-(5-carboxypentyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid | - |
Escherichia coli | |
| 1-cyclohexyl-N-(2'-hydroxy-1,1':3',1''-terphenyl-5'-yl)-5-oxopyrrolidine-3-carboxamide | - |
Escherichia coli | |
| 1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone | - |
Escherichia coli | |
| 2,4-dibromo-6-[(E)-[2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol | the binding model demonstrated that the phenolic hydroxy group of 40 interacts with the amino hydrogen of Asn247 of Escherichia coli FabH by hydrogen bonds | Escherichia coli | |
| 2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole | - |
Escherichia coli | |
| 2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole | - |
Escherichia coli | |
| 2-[4-(2,4-dinitrophenyl)-1H-pyrazol-1-yl]-4-(trifluoromethyl)pyrimidine | - |
Escherichia coli | |
| 4,5-dichloro-3H-1,2-dithiol-3-one | - |
Escherichia coli | |
| 4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol | - |
Escherichia coli | |
| 4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol | - |
Escherichia coli | |
| 5-ethyl-4-fluoro-2-[(2-fluoropyridin-3-yl)oxy]phenol | - |
Escherichia coli | |
| 5-hydroxy-2-phenyl-7-[3-(pyrrolidin-1-yl)propoxy]-2,3-dihydro-4H-chromen-4-one | a strong inhibitor, interacts with Escherichia coli FabH via a hydrogen bond between its 5-hydroxy group and the amino hydrogen of Asn247 and a hydrophobic interaction between the pyrrolidine moiety at the C7 position and Asn274, Ile 156, Phe157, and Met2 | Escherichia coli | |
| 5-[(2,6-dichlorobenzyl)oxy]-1-[(6-methyl-1,3-benzodioxol-5-yl)methyl]-1H-indole-2-carboxylic acid | - |
Escherichia coli | |
| 7-[(1E)-nonadec-1-en-1-yl]-3,4-dihydro-2H-1,5-benzodioxepine | - |
Escherichia coli | |
| acetoxyanthecotulide | - |
Escherichia coli | |
| anthecotulide | - |
Escherichia coli | |
| ethyl (2Z)-2-[4-(benzyloxy)phenyl]-3-[(4-methylphenyl)amino]prop-2-enoate | displays effective FabH inhibitory activity and excellent antibacterial activity against Gram-negative Escherichia coli. Binds to FabH through two interactions: a hydrogen bond between the N-H group and the side chain carbonyl group of Gly 209 and a hydro | Escherichia coli | |
| hydroxyanthecotulide | - |
Escherichia coli | |
| kanamycin | - |
Bacillus subtilis | |
| kanamycin | - |
Escherichia coli | |
| kanamycin | - |
Pseudomonas aeruginosa | |
| kanamycin | - |
Staphylococcus aureus | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition | Bacillus subtilis | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition. Aryl-alkyl disulfide derivatives can selectively inhibit FabH by reversibly capping the active-site cysteine through a thioldisulfide exchange | Escherichia coli | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate | Haemophilus influenzae | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate | Mycobacterium tuberculosis | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition | Pseudomonas aeruginosa | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition | Staphylococcus aureus | |
| additional information | inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate | Streptococcus pneumoniae | |
| N'-[(E)-(3,5-dibromo-2,4-dihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide | - |
Escherichia coli | |
| N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide | - |
Escherichia coli | |
| N-(3-(5-bromo-2-hydroxybenzylideneamino)propyl)-2-hydroxybenzamide | - |
Escherichia coli | |
| SB-418011 | - |
Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Streptococcus pneumoniae | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Staphylococcus aureus | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Mycobacterium tuberculosis | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Escherichia coli | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Pseudomonas aeruginosa | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Bacillus subtilis | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Haemophilus influenzae | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Staphylococcus aureus N315 | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | Mycobacterium tuberculosis H37Rv | - |
an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | O34746 | gene fabH | - |
| Escherichia coli | P0A6R0 | gene fabH | - |
| Haemophilus influenzae | P43711 | gene fabH | - |
| Mycobacterium tuberculosis | P9WNG3 | gene fabH | - |
| Mycobacterium tuberculosis H37Rv | P9WNG3 | gene fabH | - |
| Pseudomonas aeruginosa | A0A072ZQE7 | gene fabH | - |
| Staphylococcus aureus | P99159 | gene fabH | - |
| Staphylococcus aureus N315 | P99159 | gene fabH | - |
| Streptococcus pneumoniae | P0A3C5 | gene fabH | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Streptococcus pneumoniae | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Staphylococcus aureus | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Mycobacterium tuberculosis | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Escherichia coli | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Pseudomonas aeruginosa | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Bacillus subtilis | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Haemophilus influenzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Streptococcus pneumoniae | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Staphylococcus aureus | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Mycobacterium tuberculosis | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Escherichia coli | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Pseudomonas aeruginosa | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Bacillus subtilis | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Haemophilus influenzae | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | the enzyme shows a high selectivity for acetyl-CoA over acyl-ACP as its substrate. Escherichia coli FabH is inactive for longer-chain (greater than C4) primers and all branched-chain CoA primers | Escherichia coli | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Staphylococcus aureus N315 | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
| acetyl-CoA + a malonyl-[acyl-carrier protein] | - |
Mycobacterium tuberculosis H37Rv | an acetoacetyl-[acyl-carrier protein] + CoA + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | FabH has a catalytic triad of Cys112/His244/Asn274 | Staphylococcus aureus |
| More | FabH has a catalytic triad of Cys112/His244/Asn274 | Escherichia coli |
| More | FabH has a catalytic triad of Cys112/His244/Asn274 | Pseudomonas aeruginosa |
| More | FabH has a catalytic triad of Cys112/His244/Asn274 | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-ketoacyl-ACP synthase III | - |
Streptococcus pneumoniae |
| beta-ketoacyl-ACP synthase III | - |
Staphylococcus aureus |
| beta-ketoacyl-ACP synthase III | - |
Mycobacterium tuberculosis |
| beta-ketoacyl-ACP synthase III | - |
Escherichia coli |
| beta-ketoacyl-ACP synthase III | - |
Pseudomonas aeruginosa |
| beta-ketoacyl-ACP synthase III | - |
Bacillus subtilis |
| beta-ketoacyl-ACP synthase III | - |
Haemophilus influenzae |
| FabH | - |
Streptococcus pneumoniae |
| FabH | - |
Staphylococcus aureus |
| FabH | - |
Mycobacterium tuberculosis |
| FabH | - |
Escherichia coli |
| FabH | - |
Pseudomonas aeruginosa |
| FabH | - |
Bacillus subtilis |
| FabH | - |
Haemophilus influenzae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Streptococcus pneumoniae | |
| acetyl-CoA | - |
Staphylococcus aureus | |
| acetyl-CoA | - |
Mycobacterium tuberculosis | |
| acetyl-CoA | - |
Escherichia coli | |
| acetyl-CoA | - |
Pseudomonas aeruginosa | |
| acetyl-CoA | - |
Bacillus subtilis | |
| acetyl-CoA | - |
Haemophilus influenzae | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.00088 | - |
pH and temperature not specified in the publication | Escherichia coli | N-(3-(5-bromo-2-hydroxybenzylideneamino)propyl)-2-hydroxybenzamide | |
| 0.0018 | - |
pH and temperature not specified in the publication | Escherichia coli | 4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol | |
| 0.0021 | - |
pH and temperature not specified in the publication | Escherichia coli | N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide | |
| 0.0025 | - |
pH and temperature not specified in the publication | Escherichia coli | 1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate | |
| 0.0026 | - |
pH and temperature not specified in the publication | Escherichia coli | ethyl (2Z)-2-[4-(benzyloxy)phenyl]-3-[(4-methylphenyl)amino]prop-2-enoate | |
| 0.0027 | - |
pH and temperature not specified in the publication | Escherichia coli | 4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol | |
| 0.0036 | - |
pH and temperature not specified in the publication | Escherichia coli | 2,4-dibromo-6-[(E)-[2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol | |
| 0.0042 | - |
pH and temperature not specified in the publication | Escherichia coli | 1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone | |
| 0.0043 | - |
pH and temperature not specified in the publication | Escherichia coli | 1-(4-[(E)-[3-(benzyloxy)benzylidene]amino]phenyl)-3-phenylthiourea | |
| 0.0043 | - |
pH and temperature not specified in the publication | Escherichia coli | 2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole | |
| 0.0046 | - |
pH and temperature not specified in the publication | Escherichia coli | 2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole | |
| 0.0047 | - |
pH and temperature not specified in the publication | Escherichia coli | 1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Streptococcus pneumoniae |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Staphylococcus aureus |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Mycobacterium tuberculosis |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Escherichia coli |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Pseudomonas aeruginosa |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Bacillus subtilis |
| evolution | FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa | Haemophilus influenzae |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Streptococcus pneumoniae |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Staphylococcus aureus |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Mycobacterium tuberculosis |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Escherichia coli |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Pseudomonas aeruginosa |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Bacillus subtilis |
| metabolism | FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview | Haemophilus influenzae |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Streptococcus pneumoniae |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Staphylococcus aureus |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Mycobacterium tuberculosis |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Pseudomonas aeruginosa |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Bacillus subtilis |
| additional information | FabH has a catalytic triad of Cys112/His244/Asn274 | Haemophilus influenzae |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Streptococcus pneumoniae |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Staphylococcus aureus |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Mycobacterium tuberculosis |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Escherichia coli |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Pseudomonas aeruginosa |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Bacillus subtilis |
| physiological function | enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway | Haemophilus influenzae |
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