Literature summary for 5.3.1.14 extracted from

Yoshida, H.; Yamaji, M.; Ishii, T.; Izumori, K.; Kamitori, S.
Catalytic reaction mechanism of Pseudomonas stutzeri L-rhamnose isomerase deduced from X-ray structures (2010), FEBS J., 277, 1045-1057.

Search for more literature for 5.3.1.14

Application

Application	Comment	Organism
industry	as D-allose and D-psicose are rare sugars, existing in small amounts in nature, Pseudomonas stutzeri L-rhamnose isomerase is exploited for industrial applications in rare sugar production	Pseudomonas stutzeri

Cloned(Commentary)

Cloned (Comment)	Organism
a plasmid, pOI-02, encoding the L-RhI gene, is used	Pseudomonas stutzeri

Crystallization (Commentary)

Crystallization (Comment)	Organism
the structures of Mn2+-bound L-rhamnose isomerase, of the mutant S329K in complex with D-psicose or L-rhamnose, and of the mutant D327N in complex with D-psicose or L-rhamnulose are determined at resolutions of 1.8, 1.6, 1.95, 1.9, and 1.7 A, respectively	Pseudomonas stutzeri

Protein Variants

Protein Variants	Comment	Organism
D327N	inactive mutant	Pseudomonas stutzeri
S329K	inactive mutant	Pseudomonas stutzeri

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	-	Pseudomonas stutzeri
Cu2+	-	Pseudomonas stutzeri
Mn2+	-	Pseudomonas stutzeri
Zn2+	-	Pseudomonas stutzeri

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas stutzeri	Q75WH8	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas stutzeri

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-allose	-	Pseudomonas stutzeri	D-psicose	-	?
L-Rhamnose	-	Pseudomonas stutzeri	L-Rhamnulose	-	r

Subunits

Subunits	Comment	Organism
homotetramer	-	Pseudomonas stutzeri

Synonyms

Synonyms	Comment	Organism
L-rhamnose isomerase	-	Pseudomonas stutzeri

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Release 2023.1 (January 2023)