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Literature summary for 5.3.1.14 extracted from

  • Yoshida, H.; Yamada, M.; Ohyama, Y.; Takada, G.; Izumori, K.; Kamitori, S.
    The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity (2007), J. Mol. Biol., 365, 1505-1516.
    View publication on PubMed
Search for more literature for 5.3.1.14

Crystallization (Commentary)

Crystallization (Comment) Organism
purified L-RhI alone and in complexes with L-rhamnose and D-allose, X-ray diffraction structure determination and analysis at 1.97-2.0 A resolution Pseudomonas stutzeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-allose Pseudomonas stutzeri
-
 D-psicose
-
 r
L-Rhamnose Pseudomonas stutzeri
-
 L-Rhamnulose
-
 r

Organism

Organism UniProt Comment Textmining
Pseudomonas stutzeri
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-allose
-
 Pseudomonas stutzeri D-psicose
-
 r
L-Rhamnose
-
 Pseudomonas stutzeri L-Rhamnulose
-
 r
additional information substrate binding structue, overview, L-RhI can efficiently catalyze the isomerization between various aldoses and ketoses, showing a broad substrate specificity compared to L-RhI from Escherichia coli, relationship between structure and substrate specificity, overview, the beta1-alpha1 loop, Gly60Β–Arg76, of L-RhI is involved in the substrate binding of a neighbouring molecule Pseudomonas stutzeri ?
-
 ?

Subunits

Subunits Comment Organism
tetramer L-RhI has a large domain with a (beta/alpha)8 barrel fold and an additional small domain composed of seven alpha-helices, forming a homotetramer, crystal structure analysis Pseudomonas stutzeri

Synonyms

Synonyms Comment Organism
L-RhI
-
 Pseudomonas stutzeri