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Literature summary for 4.2.1.3 extracted from

  • Michta, E.; Schad, K.; Blin, K.; Ort-Winklbauer, R.; Roettig, M.; Kohlbacher, O.; Wohlleben, W.; Schinko, E.; Mast, Y.
    The bifunctional role of aconitase in Streptomyces viridochromogenes Tue494 (2012), Environ. Microbiol., 14, 3203-3219.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Streptomyces viridochromogenes

Protein Variants

Protein Variants Comment Organism
C538A mutation of cysteine residue involved in the coordination of the [4Fe-4S] cluster, mutant shows no catalytic activity. Mutant displays a lower affinity for the IRE sequence than the wild-type aconitase as shown in gel shift assays Streptomyces viridochromogenes
DELTA125-129 mutant shows lower activity compared to wild-type Streptomyces viridochromogenes
R763E/Q767E mutant shows no enzymatic activity, mutant does not bind at all to IRE-like structure as shown in gel shift assays Streptomyces viridochromogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptomyces viridochromogenes apo-AcnA is an RNA binding protein as shown in gel shift assays ?
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?

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information apo-AcnA is an RNA binding protein as shown in gel shift assays Streptomyces viridochromogenes ?
-
?

Synonyms

Synonyms Comment Organism
AcnA
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Streptomyces viridochromogenes
aconitase
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Streptomyces viridochromogenes

General Information

General Information Comment Organism
malfunction mutant shows severe defects in morphology and physiology, as is unable to form any aerial mycelium, spores or phosphinothricin tripeptide Streptomyces viridochromogenes