Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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- Name help_outline (3S)-3,6-diaminohexanoate Identifier CHEBI:57434 Charge 1 Formula C6H15N2O2 InChIKeyhelp_outline QKEWQOJCHPFEAF-YFKPBYRVSA-O SMILEShelp_outline [NH3+]CCC[C@H]([NH3+])CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (3S)-6-acetamido-3-aminohexanoate Identifier CHEBI:137165 Charge 0 Formula C8H16N2O3 InChIKeyhelp_outline MBZWIPOSTWTKSV-ZETCQYMHSA-N SMILEShelp_outline [O-]C(=O)C[C@H](CCCNC(=O)C)[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:33019 | RHEA:33020 | RHEA:33021 | RHEA:33022 | |
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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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Bacterial abl-like genes: production of the archaeal osmolyte N(epsilon)-acetyl-beta-lysine by homologous overexpression of the yodP-kamA genes in Bacillus subtilis.
Muller S., Hoffmann T., Santos H., Saum S.H., Bremer E., Muller V.
Nε-acetyl-β-lysine is an archaeal compatible solute whose synthesis is mediated by the sequential reactions of the lysine-2,3-aminomutase AblA and the acetyltransferase AblB. α-Lysine serves as the precursor and is converted by AblA to β-lysine, and AblB then acetylates this intermediate to N(ε)-a ... >> More
Nε-acetyl-β-lysine is an archaeal compatible solute whose synthesis is mediated by the sequential reactions of the lysine-2,3-aminomutase AblA and the acetyltransferase AblB. α-Lysine serves as the precursor and is converted by AblA to β-lysine, and AblB then acetylates this intermediate to N(ε)-acetyl-β-lysine. The biochemical and biophysical properties of N(ε)-acetyl-β-lysine have so far not been studied intensively due to restrictions in the supply of this compound. A search for ablAB-like genes in the genomes of members of the family Bacillaceae revealed the yodP-kamA genes that encode a AblA-related lysine-2,3-aminomutase and AblB-related putative acetyltransferase. In Bacillus subtilis, the yodP-kamA genes are part of a transcriptional unit (yodT-yodS-yodR-yodQ-yodP-kamA) whose expression is upregulated during sporulation and controlled by the mother-cell-specific transcription factor SigE. N(ε)-acetyl-β-lysine was not detectable in vegetatively growing or osmotically stressed B. subtilis cells, and the deletion of the yodT-yodS-yodR-yodQ-yodP-kamA region had no noticeable effects on growth in rich or minimal media or osmotic stress resistance. However, when we expressed the yodP-kamA genes outside their natural genetic context from an isopropyl β-D-1-thiogalactopyranoside-inducible promoter on a plasmid in B. subtilis, the recombinant strain synthesized considerable amounts (0.28 μmol/mg protein) of N(ε)-acetyl-β-lysine. The data reported here thus open the bottleneck for the large-scale production of N(ε)-acetyl-β-lysine to investigate its properties as a compatible solute. << Less
Appl. Microbiol. Biotechnol. 91:689-697(2011) [PubMed] [EuropePMC]
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Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.
Pfluger K., Baumann S., Gottschalk G., Lin W., Santos H., Muller V.
The compatible solute N(epsilon)-acetyl-beta-lysine is unique to methanogenic archaea and is produced under salt stress only. However, the molecular basis for the salt-dependent regulation of N(epsilon)-acetyl-beta-lysine formation is unknown. Genes potentially encoding lysine-2,3-aminomutase (abl ... >> More
The compatible solute N(epsilon)-acetyl-beta-lysine is unique to methanogenic archaea and is produced under salt stress only. However, the molecular basis for the salt-dependent regulation of N(epsilon)-acetyl-beta-lysine formation is unknown. Genes potentially encoding lysine-2,3-aminomutase (ablA) and beta-lysine acetyltransferase (ablB), which are assumed to catalyze N(epsilon)-acetyl-beta-lysine formation from alpha-lysine, were identified on the chromosomes of the methanogenic archaea Methanosarcina mazei Gö1, Methanosarcina acetivorans, Methanosarcina barkeri, Methanococcus jannaschii, and Methanococcus maripaludis. The order of the two genes was identical in the five organisms, and the deduced proteins were very similar, indicating a high degree of conservation of structure and function. Northern blot analysis revealed that the two genes are organized in an operon (termed the abl operon) in M. mazei Gö1. Expression of the abl operon was strictly salt dependent. The abl operon was deleted in the genetically tractable M. maripaludis. Delta(abl) mutants of M. maripaludis no longer produced N(epsilon)-acetyl-beta-lysine and were incapable of growth at high salt concentrations, indicating that the abl operon is essential for N(epsilon)-acetyl-beta-lysine synthesis. These experiments revealed the first genes involved in the biosynthesis of compatible solutes in methanogens. << Less
Appl. Environ. Microbiol. 69:6047-6055(2003) [PubMed] [EuropePMC]