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| Name | Citric Acid | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB04272 (EXPT00922) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | A key intermediate in metabolism. It is an acid compound found in citrus fruits. The salts of citric acid (citrates) can be used as anticoagulants due to their calcium chelating ability. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories |
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| CAS number | 77-92-9 | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 192.1235 Monoisotopic: 192.02700261 |
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| Chemical Formula | C6H8O7 | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=KRKNYBCHXYNGOX-UHFFFAOYSA-N | ||||||||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)
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| IUPAC Name |
2-hydroxypropane-1,2,3-tricarboxylic acid
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| SMILES |
OC(=O)CC(O)(CC(O)=O)C(O)=O
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| Manufacturers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Properties | |||||||||||||||||||||||||||||||||||||||||||
| State | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| ATC Codes |
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| AHFS Codes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| FDA label | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| MSDS | Not Available | ||||||||||||||||||||||||||||||||||||||||||
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| Drug Interactions |
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| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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1. KHG/KDPG aldolase [Includes: 4-hydroxy-2-oxoglutarate aldolase Pharmacological action: unknown4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate Organism class: bacterialUniProt ID: P0A955 ![]() Gene: eda Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 2. Molybdopterin-guanine dinucleotide biosynthesis protein A Pharmacological action: unknownLinks a guanosine 5'-phosphate to molydopterin (MPT) forming molybdopterin guanine dinucleotide (MGD) Organism class: bacterialUniProt ID: P32173 ![]() Gene: mobA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 3. Fumarate hydratase class II Pharmacological action: unknown(S)-malate = fumarate + H(2)O Organism class: bacterialUniProt ID: P05042 ![]() Gene: fumC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate Organism class: bacterialUniProt ID: Q9X0N8 ![]() Gene: pgl Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 5. Oxygen-insensitive NAD(P)H nitroreductase Pharmacological action: unknownReduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5- (aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species Organism class: bacterialUniProt ID: P38489 ![]() Gene: nfnB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
During replicative cycle of retroviruses, the reverse- transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase Organism class: viralUniProt ID: Q04095 ![]() Gene: gag-pro-pol Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: Q96RQ9 ![]() Gene: IL4I1 SNPs: SNPJam Report ![]() References:
8. Macrophage migration inhibitory factor Pharmacological action: unknownThe expression of MIF at sites of inflammation suggest a role for the mediator in regulating the function of macrophage in host defense. Also acts as a phenylpyruvate tautomerase Organism class: humanUniProt ID: P14174 ![]() Gene: MIF ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 9. Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 Pharmacological action: unknownOrganism class: human UniProt ID: Q9GZU7 ![]() Gene: CTDSP1 SNPs: SNPJam Report ![]() References:
10. 1-deoxy-D-xylulose 5-phosphate reductoisomerase Pharmacological action: unknownCatalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) Organism class: bacterialUniProt ID: P45568 ![]() Gene: dxr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 11. Tryptophan synthase alpha chain Pharmacological action: unknownThe alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3- phosphate Organism class: bacterialUniProt ID: P16608 ![]() Gene: trpA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 12. Sialidase Pharmacological action: unknownTo release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors Organism class: bacterialUniProt ID: Q02834 ![]() Gene: nedA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 13. RNASE4 protein Pharmacological action: unknownOrganism class: human UniProt ID: Q53X86 ![]() Gene: RNASE4 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: P83787 ![]() Protein Sequence: FASTA 15. Hepatocyte growth factor-regulated tyrosine kinase substrate Pharmacological action: unknownOrganism class: human UniProt ID: O14964 ![]() Gene: HGS SNPs: SNPJam Report ![]() References:
16. Invasin Pharmacological action: unknownInvasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins Organism class: bacterialUniProt ID: P11922 ![]() Gene: YPTB1668 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 17. Intron-associated endonuclease 1 Pharmacological action: unknownThis endonuclease is specific to the thymidylate synthase (td) gene splice junction and is involved in intron homing Organism class: viralUniProt ID: P13299 ![]() Gene: ITEVIR Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Structural component of the short tail fiber (baseplate) Organism class: viralUniProt ID: P10930 ![]() Gene: 12 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 19. Malate dehydrogenase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P40926 ![]() Gene: MDH2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
20. N5-carboxyaminoimidazole ribonucleotide mutase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q2QJL3 ![]() Gene: purE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Forms part of the polypeptide exit tunnel (By similarity) Organism class: bacterialUniProt ID: P38516 ![]() Gene: rplD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Preferential release of a C-terminal lysine or arginine amino acid Organism class: humanUniProt ID: P15086 ![]() Gene: CPB1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 23. Medium-chain-fatty-acid--CoA ligase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q6L8F0 ![]() Protein Sequence: FASTA Gene Sequence: FASTA 24. Hexon protein Pharmacological action: unknownThis protein is one of the structural proteins in the viral coat and is synthesized during late infection Organism class: viralUniProt ID: P03277 ![]() Gene: PII Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 25. Riboflavin kinase/FMN adenylyltransferase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WZW1 ![]() Gene: TM_0857 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Hydrolysis of sucrose, raffinose, inulin and levan. Specific for the fructose moiety and the beta-anomeric configuration of the glycosidic linkages of its substrates. The enzyme released fructose from sucrose and raffinose, and the fructose polymer inulin is hydrolyzed quantitatively in an exo- type fashion Organism class: bacterialUniProt ID: O33833 ![]() Gene: bfrA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 27. Regulator of transcription; stringent starvation protein A Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7CL96 ![]() Gene: sspA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 28. Citrate synthase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9LCX9 ![]() Gene: cit Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 29. RNA 3'-terminal phosphate cyclase Pharmacological action: unknownCatalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps:(A) adenylation of the enzyme by ATP; (B) the enzyme acts on RNA-N3'P to produce RNA-N3'PP5'A; (C) a non catalytic nucleophilic attack by the adjacent 2'hydroxyl on the phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing Organism class: bacterialUniProt ID: P46849 ![]() Gene: rtcA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 30. U6 snRNA-associated Sm-like protein LSm6 Pharmacological action: unknownOrganism class: human UniProt ID: P62312 ![]() Gene: LSM6 SNPs: SNPJam Report ![]() References:
31. Pleckstrin homology domain-containing family A member 1 Pharmacological action: unknownBinds specifically to phosphatidylinositol-3,4- diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane Organism class: humanUniProt ID: Q9HB21 ![]() Gene: PLEKHA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 32. Iron(III)-binding periplasmic protein Pharmacological action: unknownPart of the ABC transporter complex fbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (By similarity) Organism class: bacterialUniProt ID: P21408 ![]() Gene: fbpA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 33. Cell division protein FtsY Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WZ40 ![]() Gene: TM_0570 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 34. Nicotinate-nucleotide adenylyltransferase Pharmacological action: unknownCatalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity) Organism class: bacterialUniProt ID: P0A753 ![]() Gene: nadD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 35. N utilization substance protein B homolog Pharmacological action: unknownInvolved in the transcription termination process (By similarity) Organism class: bacterialUniProt ID: Q9X286 ![]() Gene: nusB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 36. Complement component C8 gamma chain Pharmacological action: unknownC8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol Organism class: humanUniProt ID: P07360 ![]() Gene: C8G Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 37. Ribonucleoside-diphosphate reductase subunit beta Pharmacological action: unknownProvides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity) Organism class: bacterialUniProt ID: Q9CBQ2 ![]() Gene: nrdF Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine Organism class: bacterialUniProt ID: P0A590 ![]() Gene: glnA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 39. Citrate synthase Pharmacological action: unknownAcetyl-CoA + H(2)O + oxaloacetate = citrate + CoA Organism class: bacterialUniProt ID: O34002 ![]() Gene: gltA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 40. Transferase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7SIC5 ![]() Protein Sequence: FASTA
Pharmacological action: unknown
Organism class: parasitic UniProt ID: Q9GV41 ![]() Gene: Tb11.02.2310 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 42. Cell division protein ftsZ Pharmacological action: unknownThis protein is essential to the cell-division process. It seems to assemble into a dynamic ring on the inner surface of the cytoplasmic membrane at the place where division will occur, and the formation of the ring is the signal for septation to begin. Binds to and hydrolyzes GTP Organism class: bacterialUniProt ID: P64170 ![]() Gene: ftsZ Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 43. Adenine phosphoribosyltransferase Pharmacological action: unknownCatalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis Organism class: humanUniProt ID: P07741 ![]() Gene: APRT ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
44. Angiogenin Pharmacological action: unknownMay function as a tRNA-specific ribonuclease that binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus, thereby promoting the endothelial invasiveness necessary for blood vessel formation. Angiogenin induces vascularization of normal and malignant tissues. Abolishes protein synthesis by specifically hydrolyzing cellular tRNAs Organism class: humanUniProt ID: P03950 ![]() Gene: ANG ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 45. Glucose-1-phosphate thymidylyltransferase Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9HU22 ![]() Gene: rmlA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Can hydrolyze carbapenem compounds Organism class: bacterialUniProt ID: P04190 ![]() Gene: blm Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q81F54 ![]() Gene: BC_1747 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine Organism class: humanUniProt ID: Q9BZX2 ![]() Gene: UCK2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 49. Tumor necrosis factor ligand superfamily member 13B Pharmacological action: unknownCytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response Organism class: humanUniProt ID: Q9Y275 ![]() Gene: TNFSF13B ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: P33644 ![]() Gene: yfiH Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 51. Betaine--homocysteine S-methyltransferase 1 Pharmacological action: unknownInvolved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline Organism class: humanUniProt ID: Q93088 ![]() Gene: BHMT ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 52. Ribose-5-phosphate isomerase A Pharmacological action: unknownD-ribose 5-phosphate = D-ribulose 5-phosphate Organism class: bacterialUniProt ID: P44725 ![]() Gene: rpiA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 53. Tryptophanyl-tRNA synthetase Pharmacological action: unknownATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp) Organism class: bacterialUniProt ID: P00953 ![]() Gene: trpS Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 54. GMP synthase [glutamine-hydrolyzing] Pharmacological action: unknownCatalyzes the synthesis of GMP from XMP Organism class: bacterialUniProt ID: P04079 ![]() Gene: guaA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 55. Aldose reductase Pharmacological action: unknownCatalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies Organism class: humanUniProt ID: P15121 ![]() Gene: AKR1B1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 56. Inosine triphosphate pyrophosphatase Pharmacological action: unknownOrganism class: human UniProt ID: Q9BY32 ![]() Gene: ITPA SNPs: SNPJam Report ![]() References:
57. Citrate synthase, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: O75390 ![]() Gene: CS SNPs: SNPJam Report ![]() References:
58. Lysozyme Pharmacological action: unknownEssential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity (By similarity) Organism class: viralUniProt ID: Q37875 ![]() Gene: 17 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 59. Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 Pharmacological action: unknownTransfers a sulfuryl group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate Organism class: humanUniProt ID: Q9Y663 ![]() Gene: HS3ST3A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 60. Glycerol uptake operon antiterminator-related protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9X1F0 ![]() Gene: TM_1436 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 61. cGMP-specific 3',5'-cyclic phosphodiesterase Pharmacological action: unknownPlays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP Organism class: humanUniProt ID: O76074 ![]() Gene: PDE5A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 62. 3-carboxy-cis,cis-muconate cycloisomerase Pharmacological action: unknownCatalyzes an anti cycloisomerization Organism class: bacterialUniProt ID: P32427 ![]() Gene: pcaB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 63. Proto-oncogene tyrosine-protein kinase Src Pharmacological action: unknownOrganism class: human UniProt ID: P12931 ![]() Gene: SRC ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
A 2-oxo acid = an aldehyde + CO(2) Organism class: bacterialUniProt ID: P06672 ![]() Gene: pdc Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA Organism class: humanUniProt ID: P07998 ![]() Gene: RNASE1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
66. Isocitrate dehydrogenase [NADP] Pharmacological action: unknownIsocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH Organism class: bacterialUniProt ID: P39126 ![]() Gene: icd Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 67. Glycine N-methyltransferase Pharmacological action: unknownCatalyzes the methylation of glycine by using S- adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine Organism class: humanUniProt ID: Q14749 ![]() Gene: GNMT ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 68. Eosinophil cationic protein Pharmacological action: unknownCytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity Organism class: humanUniProt ID: P12724 ![]() Gene: RNASE3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 69. Beta-lactamase Pharmacological action: unknownA beta-lactam + H(2)O = a substituted beta- amino acid Organism class: bacterialUniProt ID: P00808 ![]() Gene: penP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: |
| Transporters |
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1. Solute carrier organic anion transporter family member 2B1 Actions: inhibitorMediates the Na(+)-independent transport of organic anions such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene C4, thromboxane B2 and iloprost UniProt ID: O94956![]() Gene: SLCO2B1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
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