Target Information
| Target General Information | Top | |||||
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| Target ID |
T06397
(Former ID: TTDR00610)
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| Target Name |
Pseudomonas Methionine gamma-lyase (Pseudo mdeA)
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| Synonyms |
Pseudo MGL; L-methionine gamma-lyase; L-methioninase; Homocysteine desulfhydrase
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| Gene Name |
Pseudo mdeA
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| Target Type |
Literature-reported target
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[1] | ||||
| Function |
Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia. Is involved in L-methionine catabolism. In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L-homocysteine and its S-substituted derivatives, O-substituted-L-homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S-methyl-L-cysteine, and O-acetyl-L-serine. Also catalyzes deamination and gamma-addition reactions of L-vinylglycine. Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively.
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| BioChemical Class |
Carbon-sulfur lyases
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| UniProt ID | ||||||
| EC Number |
EC 4.4.1.11
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| Sequence |
MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAGHFYS
RISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDEVLLGNTLYGCTFAF LHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYFESPANPNMHMADIAGVAKIARKHG ATVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLK DMTGAVLSPHDAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQY TLARQQMSQPGGMIAFELKGGIGAGRRFMNALQLFSRAVSLGDAESLAQHPASMTHSSYT PEERAHYGISEGLVRLSVGLEDIDDLLADVQQALKASA Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Pyridoxal phosphate | Ligand Info | |||||
| Structure Description | Crystal Structure of L-methionine alpha-, gamma-lyase | PDB:1PG8 | ||||
| Method | X-ray diffraction | Resolution | 2.68 Å | Mutation | No | [3] |
| PDB Sequence |
MHGSNKLPGF
10 ATRAIHHGYD20 PQDHGGALVP30 PVYQTATFTF40 PTVEYGAACF50 AGEQAGHFYS 60 RISNPTLNLL70 EARMASLEGG80 EAGLALASGM90 GAITSTLWTL100 LRPGDEVLLG 110 NTLYGCTFAF120 LHHGIGEFGV130 KLRHVDMADL140 QALEAAMTPA150 TRVIYFESPA 160 NPNMHMADIA170 GVAKIARKHG180 ATVVVDNTYC190 TPYLQRPLEL200 GADLVVHSAT 210 KYLSGHGDIT220 AGIVVGSQAL230 VDRIRLQGLK240 DMTGAVLSPH250 DAALLMRGIK 260 TLNLRMDRHC270 ANAQVLAEFL280 ARQPQVELIH290 YPGLASFPQY300 TLARQQMSQP 310 GGMIAFELKG320 GIGAGRRFMN330 ALQLFSRAVS340 LGDAESLAQH350 PASMTHSSYT 360 PEERAHYGIS370 EGLVRLSVGL380 EDIDDLLADV390 QQALKASA
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| Ligand Name: L-homocysteine | Ligand Info | |||||
| Structure Description | Crystal structure of Pseudomonas putida methionine gamma-lyase C116H mutant with L-homocysteine intermediates. | PDB:5X30 | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | Yes | [4] |
| PDB Sequence |
> Chain A
LPGFATRAIH 16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGH 116 TFAFLHHGIG126 EFGVKLRHVD136 MADLQALEAA146 MTPATRVIYF156 ESPANPNMHM 166 ADIAGVAKIA176 RKHGATVVVD186 NTYCTPYLQR196 PLELGADLVV206 HSATYLSGHG 217 DITAGIVVGS227 QALVDRIRLQ237 GLKDMTGAVL247 SPHDAALLMR257 GIKTLNLRMD 267 RHCANAQVLA277 EFLARQPQVE287 LIHYPGLASF297 PQYTLARQQM307 SQPGGMIAFE 317 LKGGIGAGRR327 FMNALQLFSR337 AVSLGDAESL347 AQHPASMTHS357 SYTPEERAHY 367 GISEGLVRLS377 VGLEDIDDLL387 ADVQQALKAS397 A> Chain B LPGFATRAIH 16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGH 116 TFAFLHHGIG126 EFGVKLRHVD136 MADLQALEAA146 MTPATRVIYF156 ESPANPNMHM 166 ADIAGVAKIA176 RKHGATVVVD186 NTYCTPYLQR196 PLELGADLVV206 HSATKYLSGH 216 GDITAGIVVG226 SQALVDRIRL236 QGLKDMTGAV246 LSPHDAALLM256 RGIKTLNLRM 266 DRHCANAQVL276 AEFLARQPQV286 ELIHYPGLAS296 FPQYTLARQQ306 MSQPGGMIAF 316 ELKGGIGAGR326 RFMNALQLFS336 RAVSLGDAES346 LAQHPASMTH356 SSYTPEERAH 366 YGISEGLVRL376 SVGLEDIDDL386 LADVQQALKA396 SA
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Similarity Proteins
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There is no similarity protein (E value < 0.005) for this target
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| References | Top | |||||
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| REF 1 | How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6. | |||||
| REF 2 | Kinetic characterization of methionine gamma-lyases from the enteric protozoan parasite Entamoeba histolytica against physiological substrates and trifluoromethionine, a promising lead compound against amoebiasis. FEBS J. 2008 Feb;275(3):548-60. | |||||
| REF 3 | Crystal Structure of L-methionine alpha-, gamma-lyase | |||||
| REF 4 | Structural and mechanistic insights into homocysteine degradation by a mutant of methionine Gamma-lyase based on substrate-assisted catalysis. Protein Sci. 2017 Jun;26(6):1224-1230. | |||||
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