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Literature summary for 1.21.98.4 extracted from

  • Latham, J.; Iavarone, A.; Barr, I.; Juthani, P.; Klinman, J.
    PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway (2015), J. Biol. Chem., 290, 12908-12918 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
PqqD PqqD is a peptide Chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE. The stoichiometry of the MePqqD and MePqqE interaction is 1:1. PqqD is a 10 kDa protein with an unknown function, but is essential for production of pyrroloquinoline quinone Methylorubrum extorquens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a PqqA peptide + S-adenosyl-L-methionine Methylorubrum extorquens the enzyme is involved in the pyrroloquinoline quinone biosynthetic pathway. PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
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?
a PqqA peptide + S-adenosyl-L-methionine Methylorubrum extorquens ATCC 14718 the enzyme is involved in the pyrroloquinoline quinone biosynthetic pathway. PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
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?

Organism

Organism UniProt Comment Textmining
Methylorubrum extorquens P71517
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Methylorubrum extorquens ATCC 14718 P71517
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a PqqA peptide + S-adenosyl-L-methionine the enzyme is involved in the pyrroloquinoline quinone biosynthetic pathway. PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA Methylorubrum extorquens a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
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?
a PqqA peptide + S-adenosyl-L-methionine PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA Methylorubrum extorquens a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
-
?
a PqqA peptide + S-adenosyl-L-methionine the enzyme is involved in the pyrroloquinoline quinone biosynthetic pathway. PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA Methylorubrum extorquens ATCC 14718 a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
-
?
a PqqA peptide + S-adenosyl-L-methionine PqqE is a radical S-adenosylmethionine protein with a C-terminal SPASM domain, and is proposed to catalyze the formation of a carbon-carbon bond between the glutamate and tyrosine side chains of the peptide substrate PqqA Methylorubrum extorquens ATCC 14718 a PqqA peptide with linked Glu-Tyr residues + 5'-deoxyadenosine + L-methionine
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?

Synonyms

Synonyms Comment Organism
pqqE
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Methylorubrum extorquens

General Information

General Information Comment Organism
metabolism the enzyme is involved in the pyrroloquinoline quinone biosynthetic pathway Methylorubrum extorquens