Enzymes
| UniProtKB help_outline | 579 proteins |
| Enzyme class help_outline |
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- Name help_outline 5,6,7,8-tetrahydromethanopterin Identifier CHEBI:58103 Charge -3 Formula C30H42N6O16P InChIKeyhelp_outline SCBIBGUJSMHIAI-LHIIQLEZSA-K SMILEShelp_outline [H][C@]1(Nc2c(N[C@H]1C)nc(N)[nH]c2=O)[C@@H](C)Nc1ccc(C[C@H](O)[C@H](O)[C@H](O)CO[C@H]2O[C@H](COP([O-])(=O)O[C@@H](CCC([O-])=O)C([O-])=O)[C@@H](O)[C@H]2O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline formaldehyde Identifier CHEBI:16842 (Beilstein: 1209228; CAS: 50-00-0) help_outline Charge 0 Formula CH2O InChIKeyhelp_outline WSFSSNUMVMOOMR-UHFFFAOYSA-N SMILEShelp_outline [H]C([H])=O 2D coordinates Mol file for the small molecule Search links Involved in 141 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5,10-methylenetetrahydromethanopterin Identifier CHEBI:57818 Charge -3 Formula C31H42N6O16P InChIKeyhelp_outline GBMIGEWJAPFSQI-CAFBYHECSA-K SMILEShelp_outline [H][C@]12[C@H](C)Nc3nc(N)[nH]c(=O)c3N1CN([C@@H]2C)c1ccc(C[C@H](O)[C@H](O)[C@H](O)CO[C@H]2O[C@H](COP([O-])(=O)O[C@@H](CCC([O-])=O)C([O-])=O)[C@@H](O)[C@H]2O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24678 | RHEA:24679 | RHEA:24680 | RHEA:24681 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1.
Acharya P., Goenrich M., Hagemeier C.H., Demmer U., Vorholt J.A., Thauer R.K., Ermler U.
Tetrahydromethanopterin (H4 MPT) is a tetrahydrofolate analogue involved as a C1 carrier in the metabolism of various groups of microorganisms. How H4MPT is bound to the respective C1 unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activa ... >> More
Tetrahydromethanopterin (H4 MPT) is a tetrahydrofolate analogue involved as a C1 carrier in the metabolism of various groups of microorganisms. How H4MPT is bound to the respective C1 unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 established at 2.0 angstrom without and at 1.9 angstrom with methylene-H4MPT bound. Methylene-H4MPT is bound in an "S"-shaped conformation into the cleft formed between two adjacent subunits. Coenzyme binding is accompanied by side chain rearrangements up to 5 angstrom and leads to a rigidification of the C-terminal arm, a formation of a new hydrophobic cluster, and an inversion of the amide side chain of Gln88. Methylene-H4MPT in Fae shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70 degrees that is more pronounced than that reported for free methylene-H4MPT in solution (50 degrees). Fae is an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium and catalyzes the formation of methylene-H4MPT from H4MPT and formaldehyde. The molecular mechanism ofthis reaction involving His22 as acid catalyst is discussed. << Less
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Liver resections: complications and survival outcome.
Grazi G.L.
Today, liver resection represents one of the most effective therapies in the treatment of defined liver diseases, particularly for hepatocellular carcinomas, liver metastases and tumors originating from the bile ducts. There have been a number of improvements in the technique but the use of kellyc ... >> More
Today, liver resection represents one of the most effective therapies in the treatment of defined liver diseases, particularly for hepatocellular carcinomas, liver metastases and tumors originating from the bile ducts. There have been a number of improvements in the technique but the use of kellyclasia associated with meticulous control of hemostasis and biliostasis appears to be more effective and efficient. The procedure is still burdened with some postoperative complications, the more characteristic of which are liver insufficiency, biliary leakage and ascites. Several neoplastic diseases, both primitive and secondary, can benefit from this therapy with substantial improvement of long-term survival, and a notable change in the natural history of the disease. For these situations, a consultation should always be performed by a surgeon experienced in hepatic surgery. << Less
Expert Rev Pharmacoecon Outcomes Res 7:269-279(2007) [PubMed] [EuropePMC]