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Literature summary extracted from

  • Fenn, T.D.; Ringe, D.; Petsko, G.A.
    Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift (2004), Biochemistry, 43, 6464-6474.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.5 expression in Escherichia coli HB101 Streptomyces olivochromogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.5
-
 Streptomyces olivochromogenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.5 EDTA inactivates the enzyme Streptomyces olivochromogenes
5.3.1.5 xylitol
-
 Streptomyces olivochromogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.5 Mn2+ essential for activity, there are two manganese atoms visible in the atomic resolution study Streptomyces olivochromogenes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.5 D-Xylose Streptomyces olivochromogenes
-
 D-Xylulose
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.5 Streptomyces olivochromogenes P15587
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.5
-
 Streptomyces olivochromogenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.5 D-Glucose
-
 Streptomyces olivochromogenes D-Fructose
-
 r
5.3.1.5 D-Xylose
-
 Streptomyces olivochromogenes D-Xylulose
-
 r

Synonyms

EC Number Synonyms Comment Organism
5.3.1.5 xylose isomerase
-
 Streptomyces olivochromogenes