| Version |
2.5 |
| Creation Date |
2005-06-13 13:24:05 |
| Update Date |
2009-06-23 18:06:49 |
| Primary Accession Number |
DB00233 |
| Secondary Accession Number |
|
| Name |
Aminosalicylic Acid |
| Drug Type |
|
| Description |
An antitubercular agent often administered in association with isoniazid. The sodium salt of the drug is better tolerated than the free acid. [PubChem] |
| Synonyms |
- 4-ASA
- 4-aminosalicylic acid
- APAS
- Amino-PAS
- Aminosalicylate Sodium
- P-Aminosalicylic Acid
- PAS
- PASK
- Para-Amino Salicylic Acid
- Para-aminosalicylic acid
|
| Brand Names |
- Aminopar
- Aminox
- Apacil
- Deapasil
- Entepas
- Ferrosan
- Gabbropas
- Hellipidyl
- Kyselina P-Aminosalicylova
- Neopasalate
- Osacyl
- PAS-C
- Pamacyl
- Pamisyl
- Para-Pas
- Paramycin
- Parasal
- Parasalicil
- Parasalindon
- Pasa
- Pasalon
- Pasara
- Pascorbic
- Pasdium
- Pasem
- Paser
- Pasmed
- Pasnodia
- Pasolac
- Propasa
- Rezipas
- Sanipirol-4
- Sanipriol-4
|
| Brand Mixtures |
Not Available |
| Chemical IUPAC Name |
4-amino-2-hydroxybenzoic acid |
| Chemical Formula |
C7H7NO3 |
| Chemical Structure |
 |
| CAS Registry Number |
65-49-6 |
| InChI Identifier |
InChI=1/C7H7NO3/c8-4-1-2-5(7(10)11)6(9)3-4/h1-3,9H,8H2,(H,10,11)/f/h10H |
| InChI Key |
WUBBRNOQWQTFEX-KZFATGLACO |
| KEGG Drug |
D00162  |
| KEGG Compound |
C02518  |
| PubChem Compound |
4649  |
| PubChem Substance |
5528  |
| ChEBI ID |
Not Available |
| PharmGKB ID |
PA448382  |
| HET ID |
BHA  |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
Not Available |
| RxList Link |
http://www.rxlist.com/cgi/generic2/paser.htm  |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Aminosalicylic_acid  |
| FDA Label |
Not Available |
| Material Safety Data Sheet (MSDS) |
|
| Synthesis Reference |
Biniecki S., et al. Acta Pol Pharm. 1967;24(5):469-73 |
| Average Molecular Weight |
153.1354 |
| Monoisotopic Molecular Weight |
153.0426 |
| State |
Solid |
| Melting Point |
150.5 oC |
| Experimental Water Solubility |
1690 mg/L
Source: PhysProp
|
| Predicted Water Solubility |
1.18e+01 mg/mL
Calculated using ALOGPS
|
| Experimental LogP/Hydrophobicity |
1.6
Source: PhysProp
|
| Predicted LogP |
0.62
Calculated using ALOGPS
|
| Experimental LogS |
Not Available |
| Predicted LogS |
-1.11
Calculated using ALOGPS
|
| Experimental Caco2 Permeability |
Not Available |
| pKa/Isoelectric Point |
2.05 |
| Mass Spectrum |
Not Available
|
| MOL File |
Show | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
1SXK  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Isomeric SMILES |
NC1=CC(O)=C(C=C1)C(O)=O |
| Canonical SMILES |
NC1=CC(O)=C(C=C1)C(O)=O |
| Drug Category |
- Antitubercular Agents
- Antituberculosis Agents
|
| ATC Codes |
|
| AHFS Codes |
Not Available |
| Indication |
For the treatment of tuberculosis |
| Pharmacology |
Aminosalicylic acid is an anti-mycobacterial agent used with other anti-tuberculosis drugs (most often isoniazid) for the treatment of all forms of active tuberculosis due to susceptible strains of tubercle bacilli. The two major considerations in the clinical pharmacology of aminosalicylic acid are the prompt production of a toxic inactive metabolite under acid conditions and the short serum half life of one hour for the free drug. Aminosalicylic acid is bacteriostatic against Mycobacterium tuberculosis (prevents the multiplying of bacteria without destroying them). It also inhibits the onset of bacterial resistance to streptomycin and isoniazid. |
| Mechanism of Action |
There are two mechanisms responsible for aminosalicylic acid's bacteriostatic action against Mycobacterium tuberculosis. Firstly, aminosalicylic acid inhibits folic acid synthesis (without potentiation with antifolic compounds). The binding of para-aminobenzoic acid to pteridine synthetase acts as the first step in folic acid synthesis. Aminosalicylic acid binds pteridine synthetase with greater affinity than para-aminobenzoic acid, effectively inhibiting the synthesis of folic acid. As bacteria are unable to use external sources of folic acid, cell growth and multiplication slows. Secondly, aminosalicylic acid may inhibit the synthesis of the cell wall component, mycobactin, thus reducing iron uptake by M. tuberculosis. |
| Absorption |
Not Available |
| Toxicity |
LD50=4 gm/kg (orally in mice); LD50=3650 mg/kg (orally in rabbits) |
| Protein Binding |
50-60% |
| Biotransformation |
Hepatic. |
| Half Life |
Not Available |
| Dosage Forms |
|
| Patient Information |
Show  |
| Contraindications |
Show  |
| Interactions |
Show  |
| Drug Interactions |
| Drug |
Interaction |
| Azathioprine |
The 5-ASA derivative increases the toxicity of thiopurine |
| Mercaptopurine |
The 5-ASA derivative increases the toxicity of thiopurine |
| Thioguanine |
The 5-ASA derivative increases the toxicity of thiopurine |
|
| Food Interactions |
- Take without regard to meals.
|
| Pathways |
Not Available
|
| General References |
- http://www.drugs.com/mtm/aminosalicylic-acid.html
- Wikipedia

- RxList

|
| Organisms Affected |
|
| Targets |
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
- Phospholipase A2 VRV-PL-VIIIa
- P-hydroxybenzoate hydroxylase
|
|
Drug Target 1
[top]
|
| Target 1 ID |
61 |
| Target 1 Name |
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase |
| Target 1 Synonyms |
- 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
- 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
- EC 2.7.6.3
- HPPK
- PPPK
|
| Target 1 Gene Name |
folK |
| Target 1 Protein Sequence |
>2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
MTRVVLSVGSNLGDRLARLRSVADGLGDALIAASPIYEADPWGGVEQGQFLNAVLIADDP
TCEPREWLRRAQEFERAAGRVRGQRWGPRNLDVDLIACYQTSATEALVEVTARENHLTLP
HPLAHLRAFVLIPWIAVDPTAQLTVAGCPRPVTRLLAELEPADRDSVRLFRPSFDLNSRH
PVSRAPES
|
| Target 1 Number of Residues |
191 |
| Target 1 Molecular Weight |
20732 |
| Target 1 Theoretical pI |
6.12 |
| Target 1 GO Classification |
|
Function
|
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity |
|
Process
|
physiological process
metabolism
cellular metabolism
aromatic compound metabolism
folic acid and derivative metabolism
folic acid and derivative biosynthesis |
|
Component
|
| Not Available |
|
| Target 1 General Function |
Coenzyme transport and metabolism |
| Target 1 Specific Function |
Not Available |
| Target 1 Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Folate biosynthesis |
|
map00790  |
|
| Target 1 Reactions |
- ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
|
| Target 1 Pfam Domain Function |
|
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
|
| Target 1 Essentiality |
Essential |
| Target 1 GenBank ID Protein |
2113971  |
| Target 1 UniProtKB/Swiss-Prot ID |
P64143  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
HPPK_MYCTU  |
| Target 1 PDB ID |
Not Available |
| Target 1 Cellular Location |
Not Available |
| Target 1 Gene Sequence |
>567 bp
TCAGCTTTCCGGTGCCCGACTGACGGGGTGTCTGCTATTCAGATCGAACGACGGCCTAAA
CAACCGCACACTGTCGCGGTCGGCGGGCTCCAGCTCGGCCAGCAGTCGCGTGACGGGCCG
CGGGCACCCGGCAACCGTCAGCTGCGCCGTTGGGTCGACGGCAATCCACGGGATCAACAC
AAAGGCCCGCAGATGCGCCAGTGGGTGCGGCAGCGTGAGGTGGTTCTCCCGCGCGGTCAC
TTCGACCAGAGCCTCGGTGGCCGAGGTCTGGTAGCAGGCGATCAGGTCGACGTCGAGATT
TCGTGGACCCCAGCGCTGGCCACGCACCCTGCCCGCAGCGCGCTCGAACTCCTGCGCCCG
CCGCAGCCACTCCCGCGGTTCGCAGGTAGGATCGTCGGCGATCAGCACCGCATTGAGGAA
CTGCCCCTGCTCCACCCCACCCCAGGGGTCGGCCTCATATATCGGGGAAGCCGCAATCAA
CGCATCGCCGAGACCGTCGGCGACCGACCGCAATCGTGCCAGGCGGTCACCCAGGTTGGA
GCCAACCGAGAGCACTACCCGCGTCAT
|
| Target 1 GenBank Gene ID |
|
| Target 1 GeneCard ID |
Not Available |
| Target 1 GenAtlas ID |
Not Available |
| Target 1 HGNC ID |
Not Available |
| Target 1 Chromosome Location |
Not Available |
| Target 1 Locus |
Not Available |
| Target 1 SNPs |
SNPJam Report  |
| Target 1 General References |
- Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed
]
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed
]
|
| Target 1 Drug References |
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
|
|
Drug Target 2
[top]
|
| Target 2 ID |
2394 |
| Target 2 Name |
Phospholipase A2 VRV-PL-VIIIa |
| Target 2 Synonyms |
- DPLA2
- EC 3.1.1.4
- Phosphatidylcholine 2- acylhydrolase
|
| Target 2 Gene Name |
Not Available |
| Target 2 Protein Sequence |
>Phospholipase A2 VRV-PL-VIIIa
SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDATDRCCFVHDCCYGNLPDCNPK
SDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELK
C
|
| Target 2 Number of Residues |
123 |
| Target 2 Molecular Weight |
13611 |
| Target 2 Theoretical pI |
8.06 |
| Target 2 GO Classification |
|
Function
|
binding
ion binding
cation binding
calcium ion binding
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
carboxylic ester hydrolase activity
lipase activity
phospholipase activity
phospholipase A2 activity |
|
Process
|
physiological process
metabolism
primary metabolism
lipid metabolism
lipid catabolism |
|
Component
|
| Not Available |
|
| Target 2 General Function |
Involved in phospholipase A2 activity |
| Target 2 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This toxin shows neurotoxic symptoms and damages vital organs such as lung, liver and kidney. Displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle |
| Target 2 Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Glycerophospholipid metabolism |
|
map00564  |
|
| Target 2 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
|
| Target 2 Pfam Domain Function |
|
| Target 2 Signals |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Essential |
| Target 2 GenBank ID Protein |
Not Available |
| Target 2 UniProtKB/Swiss-Prot ID |
P59071  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
PA28_DABRP  |
| Target 2 PDB ID |
1Y38  |
| Target 2 PDB File |
Show |
| Target 2 3D Structure |
|
| Target 2 Cellular Location |
|
| Target 2 Gene Sequence |
Not Available |
| Target 2 GenBank Gene ID |
|
| Target 2 GeneCard ID |
Not Available |
| Target 2 GenAtlas ID |
Not Available |
| Target 2 HGNC ID |
Not Available |
| Target 2 Chromosome Location |
Not Available |
| Target 2 Locus |
Not Available |
| Target 2 SNPs |
Not Available |
| Target 2 General References |
- Kasturi S, Gowda TV: Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom. Toxicon. 1989;27(2):229-37. [PubMed
]
- Gowda VT, Schmidt J, Middlebrook JL: Primary sequence determination of the most basic myonecrotic phospholipase A2 from the venom of Vipera russelli. Toxicon. 1994 Jun;32(6):665-73. [PubMed
]
|
| Target 2 Drug References |
Not Available |
|
Drug Target 3
[top]
|
| Target 3 ID |
2769 |
| Target 3 Name |
P-hydroxybenzoate hydroxylase |
| Target 3 Synonyms |
- 4-hydroxybenzoate 3- monooxygenase
- EC 1.14.13.2
|
| Target 3 Gene Name |
pobA |
| Target 3 Protein Sequence |
>P-hydroxybenzoate hydroxylase
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAG
VDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATT
VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERV
YPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLN
LAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS
QRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
|
| Target 3 Number of Residues |
400 |
| Target 3 Molecular Weight |
44322 |
| Target 3 Theoretical pI |
6.80 |
| Target 3 GO Classification |
|
Function
|
catalytic activity
oxidoreductase activity
monooxygenase activity |
|
Process
|
aromatic compound metabolism
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport |
|
Component
|
| Not Available |
|
| Target 3 General Function |
Coenzyme transport and metabolism |
| Target 3 Specific Function |
4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O |
| Target 3 Pathways |
| Name |
SMPDB Link |
KEGG Link |
| Benzoate degradation via hydroxylation |
|
map00362  |
|
| Target 3 Reactions |
- 4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O
|
| Target 3 Pfam Domain Function |
|
| Target 3 Signals |
|
| Target 3 Transmembrane Regions |
|
| Target 3 Essentiality |
Essential |
| Target 3 GenBank ID Protein |
49145  |
| Target 3 UniProtKB/Swiss-Prot ID |
P00438  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
PHHY_PSEFL  |
| Target 3 PDB ID |
2PHH  |
| Target 3 PDB File |
Show |
| Target 3 3D Structure |
|
| Target 3 Cellular Location |
Not Available |
| Target 3 Gene Sequence |
>1185 bp
ATGAAGACTCAAGTCGCCATCATCGGCGCCGGTCCGTCCGGCCTCCTGCTCGGCCAGTTG
CTGCACAAGGCCGGCATCGACAACGTGATCCTCGAACGCCAGACCCCGGACTACGTGCTC
GGCCGCATCCGCGCCGGCGTGCTGGAACAGGGTATGGTCGACCTGCTGCGCGAGGCCGGC
GTCGACCGGCGCATGGCGCGCGACGGGCTGGTCCACGAAGGCGTGGAGATCGCCTTCGCC
GGGCAGCGCCGGCGCATCGACCTGAAGCGCCTGAGCGGCGGCAAGACGGTGACGGTCTAC
GGCCAGACCGAGGTCACCCGCGACCTCATGGAAGCCCGCGAAGCCTGCGGCGCCACTACC
GTCTACCAGGCCGCCGAGGTGCGCCTGCACGACCTGCAAGGTGAGCGCCCCTACGTGACC
TTCGAACGCGACGGCGAACGGCTACGCCTGGATTGCGACTACATCGCCGGCTGCGATGGC
TTCCACGGCATCTCGCGGCAATCGATCCCGGCGGAGCGGCTGAAGGTCTTCGAGCGGGTC
TATCCGTTCGGCTGGCTCGGCCTGCTCGCCGACACCCCGCCGGTCAGCCACGAACTGATC
TACGCCAACCATCCGCGCGGCTTCGCCCTGTGCAGCCAGCGTTCGGCGACCCGCAGCCGC
TACTACGTACAGGTGCCATTGACAGAGAAGGTCGAGGACTGGTCCGACGAGCGCTTCTGG
ACGGAACTGAAAGCGCGCCTCCCGGCCGAGGTGGCGGAGAAACTGGTGACCGGTCCTTCG
CTGGAGAAGAGCATCGCGCCGCTGCGCAGCTTCGTGGTCGAGCCGATGCAGCATGGCCGG
CTGTTCCTCGCCGGCGACGCCGCGCACATCGTGCCGCCCACCGGCGCCAAGGGACTGAAC
CTGGCGGCCAGCGACGTCAGCACGCTCTACCGGCTGCTGCTGAAGGCCTACCGCGAAGGG
CGGGGCGAACTGCTGGAACGCTACTCGGCAATCTGCCTGCGGCGGATCTGGAAGGCCGAA
CGCTTCTCCTGGTGGATGACTTCGGTGCTGCATCGCTTCCCCGACACCGACGCGTTCAGC
CAGCGCATCCAGCAGACCGAACTGGAGTACTACCTGGGCTCCGAGGCGGGCCTGGCGACC
ATCGCCGAGAACTATGTCGGCCTGCCCTACGAGGAAATCGAGTAG
|
| Target 3 GenBank Gene ID |
|
| Target 3 GeneCard ID |
Not Available |
| Target 3 GenAtlas ID |
Not Available |
| Target 3 HGNC ID |
Not Available |
| Target 3 Chromosome Location |
Not Available |
| Target 3 Locus |
Not Available |
| Target 3 SNPs |
SNPJam Report  |
| Target 3 General References |
- Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ: Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. FEBS Lett. 1999 Jan 29;443(3):251-5. [PubMed
]
- Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J: Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution. Proteins. 1992 Oct;14(2):178-90. [PubMed
]
- van Berkel W, Westphal A, Eschrich K, Eppink M, de Kok A: Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur J Biochem. 1992 Dec 1;210(2):411-9. [PubMed
]
- Schreuder HA, van der Laan JM, Hol WG, Drenth J: Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate. J Mol Biol. 1988 Feb 20;199(4):637-48. [PubMed
]
- Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J: Crystal structure of p-hydroxybenzoate hydroxylase. J Mol Biol. 1979 Jun 15;131(1):55-73. [PubMed
]
- Weijer WJ, Hofsteenge J, Beintema JJ, Wierenga RK, Drenth J: p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure. Eur J Biochem. 1983 Jun 1;133(1):109-18. [PubMed
]
- Hofsteenge J, Weijer WJ, Jekel PA, Beintema JJ: p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 1. Completion of the elucidation of the primary structure. Eur J Biochem. 1983 Jun 1;133(1):91-108. [PubMed
]
- Hofsteenge J, Vereijken JM, Weijer WJ, Beintema JJ, Wierenga RK, Drenth J: Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide. Eur J Biochem. 1980 Dec;113(1):141-50. [PubMed
]
- Vereijken JM, Hofsteenge J, Bak HJ, Beintema JJ: The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur J Biochem. 1980 Dec;113(1):151-7. [PubMed
]
- Weijer WJ, Hofsteenge J, Vereijken JM, Jekel PA, Beintema JJ: Primary structure of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Biochim Biophys Acta. 1982 Jun 4;704(2):385-8. [PubMed
]
- 7628466 Eppink MH, Schreuder HA, Van Berkel WJ: Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding. Eur J Biochem. 1995 Jul 1;231(1):157-65.
- 9578477 Eppink MH, Schreuder HA, van Berkel WJ: Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. Eur J Biochem. 1998 Apr 1;253(1):194-201.
|
| Target 3 Drug References |
Not Available |