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Literature summary extracted from

  • Yakobov, N.; Fischer, F.; Mahmoudi, N.; Saga, Y.; Grube, C.D.; Roy, H.; Senger, B.; Grob, G.; Tatematsu, S.; Yokokawa, D.; Mouyna, I.; Latge, J.-P.; Nakajima, H.; Kushiro, T.; Becker, H.D.
    RNA-dependent sterol aspartylation in fungi (2020), Proc. Natl. Acad. Sci. USA, 117, 14948-14957 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.B13 D277A mutation in predicted catalytic triad, inactive Aspergillus fumigatus
3.1.1.B13 H307A mutation in predicted catalytic triad, inactive Aspergillus fumigatus
3.1.1.B13 S153A mutation in predicted catalytic triad, inactive Aspergillus fumigatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.B17 ATP + Asp + ergosterol Aspergillus oryzae
-
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + ergosterol Aspergillus oryzae ATCC 42149
-
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + tRNAAsn Aspergillus oryzae
-
AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ATP + Asp + tRNAAsn Aspergillus oryzae ATCC 42149
-
AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn Aspergillus oryzae
-
ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn Aspergillus oryzae ATCC 42149
-
ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 additional information Aspergillus oryzae a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol ?
-
-
2.3.2.B17 additional information Aspergillus oryzae ATCC 42149 a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol ?
-
-
3.1.1.B13 ergosteryl-3beta-O-L-aspartate + H2O Aspergillus oryzae
-
ergosterol + L-aspartate
-
?
3.1.1.B13 ergosteryl-3beta-O-L-aspartate + H2O Aspergillus fumigatus
-
ergosterol + L-aspartate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.B17 Aspergillus fumigatus Q4WKG3 cf. EC 6.1.1.12
-
2.3.2.B17 Aspergillus fumigatus ATCC MYA-4609 Q4WKG3 cf. EC 6.1.1.12
-
2.3.2.B17 Aspergillus oryzae Q2URG4 cf. EC 6.1.1.12
-
2.3.2.B17 Aspergillus oryzae ATCC 42149 Q2URG4 cf. EC 6.1.1.12
-
3.1.1.B13 Aspergillus fumigatus
-
-
-
3.1.1.B13 Aspergillus oryzae
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.B17 mycelium
-
Aspergillus oryzae
-
2.3.2.B17 mycelium
-
Aspergillus fumigatus
-
3.1.1.B13 mycelium
-
Aspergillus oryzae
-
3.1.1.B13 mycelium
-
Aspergillus fumigatus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.B17 ATP + Asp + ergosterol
-
Aspergillus oryzae AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + ergosterol
-
Aspergillus fumigatus AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + ergosterol
-
Aspergillus fumigatus ATCC MYA-4609 AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + ergosterol
-
Aspergillus oryzae ATCC 42149 AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + Asp + tRNAAsn
-
Aspergillus oryzae AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ATP + Asp + tRNAAsn
-
Aspergillus fumigatus AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ATP + Asp + tRNAAsn
-
Aspergillus fumigatus ATCC MYA-4609 AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ATP + Asp + tRNAAsn
-
Aspergillus oryzae ATCC 42149 AMP + diphosphate + L-aspartyl-tRNAAsn
-
?
2.3.2.B17 ATP + L-aspartate + ergosterol
-
Aspergillus oryzae AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ATP + L-aspartate + ergosterol
-
Aspergillus oryzae ATCC 42149 AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn
-
Aspergillus oryzae ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn
-
Aspergillus fumigatus ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn
-
Aspergillus fumigatus ATCC MYA-4609 ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 ergosterol + L-aspartyl-tRNAAsn
-
Aspergillus oryzae ATCC 42149 ergosteryl-3beta-O-L-aspartate + tRNAAsn
-
?
2.3.2.B17 additional information a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol Aspergillus oryzae ?
-
-
2.3.2.B17 additional information a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol Aspergillus fumigatus ?
-
-
2.3.2.B17 additional information a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol Aspergillus fumigatus ATCC MYA-4609 ?
-
-
2.3.2.B17 additional information a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol Aspergillus oryzae ATCC 42149 ?
-
-
3.1.1.B13 ergosteryl-3beta-O-L-aspartate + H2O
-
Aspergillus oryzae ergosterol + L-aspartate
-
?
3.1.1.B13 ergosteryl-3beta-O-L-aspartate + H2O
-
Aspergillus fumigatus ergosterol + L-aspartate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.B17 AFUA_1g02570
-
Aspergillus fumigatus
2.3.2.B17 AO090005000838
-
Aspergillus oryzae
2.3.2.B17 DUF2156 domain protein
-
Aspergillus oryzae
2.3.2.B17 DUF2156 domain protein
-
Aspergillus fumigatus
2.3.2.B17 ErdS
-
Aspergillus oryzae
2.3.2.B17 ErdS
-
Aspergillus fumigatus
2.3.2.B17 ergosteryl-3beta-O-L-aspartate synthase
-
Aspergillus oryzae
2.3.2.B17 ergosteryl-3beta-O-L-aspartate synthase
-
Aspergillus fumigatus
3.1.1.B13 ErdH
-
Aspergillus oryzae
3.1.1.B13 ErdH
-
Aspergillus fumigatus
3.1.1.B13 ergosteryl-3beta-O-L-aspartate hydrolase
-
Aspergillus oryzae
3.1.1.B13 ergosteryl-3beta-O-L-aspartate hydrolase
-
Aspergillus fumigatus

General Information

EC Number General Information Comment Organism
2.3.2.B17 evolution ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi Aspergillus oryzae
2.3.2.B17 evolution ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi Aspergillus fumigatus
2.3.2.B17 physiological function ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdS enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo Aspergillus fumigatus
2.3.2.B17 physiological function ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdSs enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo Aspergillus oryzae
3.1.1.B13 physiological function ErdH is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo Aspergillus oryzae
3.1.1.B13 physiological function ErdH is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo Aspergillus fumigatus