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Literature summary for 5.4.3.6 extracted from

  • Cooke, H.A.; Bruner, S.D.
    Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites (2010), Biopolymers, 93, 802-810.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Streptomyces globisporus

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme E71A using 100 mM trimethylamine N-oxide, 4.6 M sodium formate, at 4°C, and mutant enzyme Y63F using 95 mM trimethylamine N-oxide, 4.6 M sodium formate with 2 mM L-tyrosine, at 20°C Streptomyces globisporus

Protein Variants

Protein Variants Comment Organism
E71A the mutant has a significant decrease in activity Streptomyces globisporus
H93F the mutant has no activity with L-phenylalanine and L-tyrosine Streptomyces globisporus
Y415F/H93 the mutant has no activity with L-phenylalanine Streptomyces globisporus
Y63F completely inactive Streptomyces globisporus

Organism

Organism UniProt Comment Textmining
Streptomyces globisporus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration Streptomyces globisporus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine
-
 Streptomyces globisporus (S)-beta-tyrosine
-
 r

Synonyms

Synonyms Comment Organism
TAM
-
 Streptomyces globisporus
tyrosine aminomutase
-
 Streptomyces globisporus