5.3.1.14: L-rhamnose isomerase
This is an abbreviated version!
For detailed information about L-rhamnose isomerase, go to the full flat file.
Word Map on EC 5.3.1.14
-
5.3.1.14
-
l-rhamnulose
-
d-allose
-
isomerization
-
d-psicose
-
3-epimerase
-
isomerases
-
stutzeri
-
rhaas
-
l-lyxose
-
synthesis
-
isomerized
-
aldoses
-
l-xylulose
-
ketoses
-
l-mannose
-
l-tagatose
-
caldicellulosiruptor
-
l-ribose
-
l-galactose
-
epimerized
-
industry
-
food industry
- 5.3.1.14
- l-rhamnulose
- d-allose
-
isomerization
- d-psicose
-
3-epimerase
- isomerases
- stutzeri
-
rhaas
- l-lyxose
- synthesis
-
isomerized
- aldoses
- l-xylulose
- ketoses
- l-mannose
- l-tagatose
-
caldicellulosiruptor
- l-ribose
- l-galactose
-
epimerized
- industry
- food industry
Reaction
Synonyms
COB47_0655, Isomerase, L-rhamnose, L-rhamnose isomerase, L-rhamnose ketol-isomerase, L-RhI, L-RI, RhaA, RhaI, Rhamnose isomerase
ECTree
5.3.1.14 L-rhamnose isomeraseAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 5.3.1.14 - L-rhamnose isomerase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
the enzyme shows 1% activity in the presence of 1 mM Ca2+ as compared to 1 mM Co2+
Co2+
Mg2+
Mn2+
Na+
the enzyme shows 19% activity in the presence of 1 mM Na+ as compared to 1 mM Co2+
Ni2+
Zn2+
additional information
Co2+
Halalkalibacterium halodurans
-
required for catalytic activity, 93% activity at 1 mM compared to Mn2+
Mg2+
Halalkalibacterium halodurans
-
required for catalytic activity, 57% activity at 1 mM compared to Mn2+
Mg2+
the enzyme shows 9% activity in the presence of 1 mM Mg2+ as compared to 1 mM Co2+
Mn2+
the enzyme shows 58% of the maximum activity in the presence of Mn2+
Mn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
Mn2+
the enzyme shows 61% activity in the presence of 1 mM Mn2+ as compared to 1 mM Co2+
Mn2+
1 mM, optimum concentration, 7fold increase in activity
Mn2+
-
enzyme activity is the highest with Mn2+, the optimal Mn2+ concentration is 1 mM (6.7fold increase activity relative to no treatment)
Zn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
Zn2+
Halalkalibacterium halodurans
-
required for catalytic activity, 20% activity at 1 mM compared to Mn2+
Zn2+
the enzyme shows 2% activity in the presence of 1 mM Zn2+ as compared to 1 mM Co2+
additional information
no activity in the presence of Na+, Mg2+, Ca2+, Cu2+, K+, and Zn2+ or in the absence of any ions
additional information
-
no activity in the presence of Na+, Mg2+, Ca2+, Cu2+, K+, and Zn2+ or in the absence of any ions
additional information
Halalkalibacterium halodurans
-
enzyme without any metal ions shows a negligible activity. The enzyme activity is not stimulated by Ca2+, Ba2+, Na2+, Fe2+, or Cu2+
additional information
the enzyme shows null activity in the absence of any ions, as well as in the presence of Cu2+ and K+
additional information
-
the enzyme shows null activity in the absence of any ions, as well as in the presence of Cu2+ and K+
