Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline 3-(4-hydroxyphenyl)pyruvate Identifier CHEBI:36242 (Beilstein: 3950858) help_outline Charge -1 Formula C9H7O4 InChIKeyhelp_outline KKADPXVIOXHVKN-UHFFFAOYSA-M SMILEShelp_outline Oc1ccc(CC(=O)C([O-])=O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 20 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline aspulvinone E Identifier CHEBI:58240 Charge -1 Formula C17H11O5 InChIKeyhelp_outline BNNVVTQUWNGKPH-ZROIWOOFSA-M SMILEShelp_outline Oc1ccc(cc1)\C=C1OC(=O)C(=C/1[O-])c1ccc(O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 5 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:63824 | RHEA:63825 | RHEA:63826 | RHEA:63827 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Production of alpha-keto carboxylic acid dimers in yeast by overexpression of NRPS-like genes from Aspergillus terreus.
Huehner E., Backhaus K., Kraut R., Li S.M.
Non-ribosomal peptide synthetases (NRPSs) are key enzymes in microorganisms for the assembly of peptide backbones of biologically and pharmacologically active natural products. The monomodular NRPS-like enzymes comprise often an adenylation (A), a thiolation (T), and a thioesterase (TE) domain. In ... >> More
Non-ribosomal peptide synthetases (NRPSs) are key enzymes in microorganisms for the assembly of peptide backbones of biologically and pharmacologically active natural products. The monomodular NRPS-like enzymes comprise often an adenylation (A), a thiolation (T), and a thioesterase (TE) domain. In contrast to the NRPSs, they do not contain any condensation domain and usually catalyze a dimerization of α-keto carboxylic acids and thereby provide diverse scaffolds for further modifications. In this study, we established an expression system for NRPS-like genes in Saccharomyces cerevisiae. By expression of four known genes from Aspergillus terreus, their predicted function was confirmed and product yields of up to 35 mg per liter culture were achieved. Furthermore, expression of ATEG_03090 from the same fungus, encoding for the last uncharacterized NRPS-like enzyme with an A-T-TE domain structure, led to the formation of the benzoquinone derivative atromentin. All the accumulated products were isolated and their structures were elucidated by NMR and MS analyses. This study provides a convenient system for proof of gene function as well as a basis for synthetic biology, since additional genes encoding modification enzymes can be introduced. << Less
Appl. Microbiol. Biotechnol. 102:1663-1672(2018) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.