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Literature summary for 4.2.1.3 extracted from

  • Williams, C.H.; Stillman, T.J.; Barynin, V.V.; Sedelnikova, S.E.; Tang, Y.; Green, J.; Guest, J.R.; Artymiuk, P.J.
    E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition (2002), Nat. Struct. Biol., 9, 447-452.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
2.4 A structure of AcnB, hanging drop vapor diffusion at 17°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the HEAT-like domain, implies a role in protein-protein recognition ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P36683
-
-

Purification (Commentary)

Purification (Comment) Organism
native and SeMet [3Fe-4S] form of AcnB expressed in Escherichia coli Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the HEAT-like domain, implies a role in protein-protein recognition Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
AcnB
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Escherichia coli