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Ligand L-rhamnopyranose

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

degradation of hexoses

KEGG

Fructose and mannose metabolism, Microbial metabolism in diverse environments

MetaCyc

L-rhamnose degradation I, L-rhamnose degradation II, L-rhamnose degradation III, rhamnogalacturonan type I degradation I, rhamnogalacturonan type I degradation II (bacteria), rutin degradation (plants) more

Show all BRENDA pathways known for L-rhamnopyranose

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Natural Substrate (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.173

L-rhamnose + NAD+ = L-rhamno-1,4-lactone + NADH

347732, 347733, 347736, 687737, 686697

-

1.1.1.377

L-rhamnose + NADP+ = L-rhamno-1,4-lactone + NADPH + H+

727435

-

1.1.1.378

L-rhamnose + NAD(P)+ = L-rhamno-1,4-lactone + NAD(P)H + H+

687737

-

1.1.1.378

L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+

697897

-

1.1.1.378

L-rhamnose + NADP+ = L-rhamnono-1,4-lactone + NADPH + H+

763033

-

5.3.1.14

L-rhamnopyranose = L-rhamnulose

769709

-

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

1DE6, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

2I56, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

3ITT, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

3M0H, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

3M0V, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

3M0Y, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

677350, 677768, 680947, 681406, 703677, 705332, 727230, 727653, 727537, 769709, 772450, 773107, 747394, 748497

4GJI, 3D-view

1.1.1.378

3 entries

5.3.1.14

8 entries

5.3.1.6

L-Rhamnose = L-Rhamnulose

773509

-

In Vivo Product in Enzyme-catalyzed Reactions (29 results)

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Show Natural Product (29 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.247

beta-D-galactosyl-(1->4)-L-rhamnose + phosphate = L-rhamnose + alpha-D-galactose 1-phosphate

-

-

3.2.1.172

2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 4-deoxy-alpha-L-threo-hex-4-enopyranuronate + L-rhamnopyranose

-

-

3.2.1.172

2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose

-

-

3.2.1.172

2 entries

3.2.1.189

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O = D-glucopyranose + 2 L-rhamnopyranose + diosgenin

-

-

3.2.1.190

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 2 H2O = 2 L-rhamnopyranose + diosgenin 3-O-beta-D-glucopyranoside

-

-

3.2.1.192

ginsenoside Re + H2O = ginsenoside Rg2 + L-rhamnose

-

-

3.2.1.194

ginsenoside R1 + H2O = ginsenoside F1 + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside F1 + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside Rg1 + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside Rg2 + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + 2 H2O = protopanaxatriol + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + H2O = ginsenoside Rh1 + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + H2O = protopanaxatriol + D-glucose + L-rhamnose

-

-

3.2.1.194

7 entries

3.2.1.195

ginsenoside Re + H2O = ginsenoside Rh1 + D-glucose + L-rhamnose

-

-

3.2.1.24

mannosyl rhamnose + H2O = alpha-D-mannopyranose + rhamnose

136025

-

3.2.1.40

epimedin C + H2O = icariin + L-rhamnose

-

-

3.2.1.40

epoetin C + H2O = icariin + L-rhamnose

-

-

3.2.1.40

hesperidin + H2O = ? + L-rhamnose

-

-

3.2.1.40

hesperidin + H2O = hesperetin-7-O-glucoside + L-rhamnose

-

-

3.2.1.40

naringin + H2O = ? + L-rhamnose

-

-

3.2.1.40

naringin + H2O = prunin + L-rhamnose

-

-

3.2.1.40

neohesperidin + H2O = hesperetin-7-O-glucoside + L-rhamnose

-

-

3.2.1.40

quercitrin + H2O = ? + L-rhamnose

-

-

3.2.1.40

quercitrin + H2O = quercetin + L-rhamnose

136772, -

-

3.2.1.40

rutin + H2O = ? + L-rhamnose

-

-

3.2.1.40

rutin + H2O = isoquercetin + L-rhamnose

-

-

3.2.1.40

rutin + H2O = quercetin-3-beta-D-glucoside + L-rhamnose

-

-

3.2.1.40

12 entries

3.2.1.B31

quercitrin + H2O = quercetin + L-rhamnose

-

-

5.3.1.14

L-rhamnulose = L-rhamnopyranose

-

-

Substrate in Enzyme-catalyzed Reactions (40 results)

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Show Substrate (40 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.14

L-rhamnose + NADH = ?

285901

-

1.1.1.173

L-rhamnose + NAD+ = L-rhamno-1,4-lactone + NADH

347732, 347733, 286118, 347736, 687737, 686697, 733813

-

1.1.1.173

L-rhamnose + NAD+ = L-rhamno-1,4-lactone + NADH + H+

765347

-

1.1.1.173

L-rhamnose + NADP+ = L-rhamno-1,4-lactone + NADPH

733813

-

1.1.1.173

3 entries

1.1.1.21

L-rhamnose + NADPH = L-rhamnitol + NADP+

286255

-

1.1.1.377

L-rhamnose + NADP+ = L-rhamno-1,4-lactone + NADPH + H+

727435

-

1.1.1.378

L-rhamnose + NAD(P)+ = L-rhamno-1,4-lactone + NAD(P)H + H+

687737

-

1.1.1.378

L-rhamnose + NAD(P)+ = L-rhamnono-1,4-lactone + NAD(P)H + H+

697897

-

1.1.1.378

L-rhamnose + NAD+ = L-rhamno-1,4-lactone + NADH + H+

687737

-

1.1.1.378

L-rhamnose + NAD+ = L-rhamnono-1,4-lactone + NADH + H+

697897, 763033

-

1.1.1.378

L-rhamnose + NADP+ = L-rhamno-1,4-lactone + NADPH + H+

687737

-

1.1.1.378

L-rhamnose + NADP+ = L-rhamnono-1,4-lactone + NADPH + H+

697897, 763033

-

1.1.1.378

6 entries

1.1.2.B5

L-rhamnose + 2,6-dichlorophenolindophenol = ? + reduced 2,6-dichlorophenolindophenol

741228

-

1.1.5.2

L-rhamnose + pyrroloquinoline quinone = L-rhamnono-1,5-lactone + pyrroloquinoline quinol

639203, 639191

-

1.1.5.9

L-rhamnose + acceptor = L-rhamnone-1,5-lactone + reduced acceptor

348276

-

1.2.1.92

L-rhamnose + NADP+ + H2O = ?

763358

-

2.2.1.1

2-hydroxypyruvate + 6-deoxy-L-mannose = 8-deoxy-L-glycero-L-galacto-octulose

777071

-

2.4.1.13

UDP-alpha-D-glucose + L-rhamnose = ?

703490

-

2.4.1.162

sucrose + L-rhamnose = D-glucose + beta-D-fructofuranosyl-(2,1)-L-rhamnoside

692116

-

2.4.1.162

sucrose + L-rhamnose = D-glucose + beta-D-fructofuranosyl-(2->1)-L-rhamnoside

488677

-

2.4.1.247

alpha-D-galactose 1-phosphate + L-rhamnose = D-galactosyl-beta-1,4-L-rhamnose + phosphate

693235

-

2.4.1.247

L-rhamnose + alpha-D-galactose 1-phosphate = beta-D-galactosyl-(1->4)-L-rhamnose + phosphate

722132

-

2.4.1.162

2 entries

2.4.1.247

2 entries

2.4.1.282

L-rhamnose + beta-D-glucose 1-phosphate = 3-O-alpha-D-glucopyranosyl-L-rhamnopyranose + phosphate

714662

-

2.4.1.7

sucrose + rhamnose = ?

679550

-

2.7.1.52

ATP + L-rhamnose = ?

641670

-

3.2.1.23

lactose + rhamnose = ?

171351

-

3.2.1.40

2'-deoxy-5-fluorouridine + L-rhamnose = ?

768771

-

3.2.1.40

cytosine arabinoside + L-rhamnose = ?

768771

-

3.2.1.40

hydroxyurea + L-rhamnose = ?

768771

-

5.3.1.14

L-rhamnopyranose = L-rhamnulose

769709

-

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

1DE6, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

2I56, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

3ITT, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

3M0H, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

3M0V, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

3M0Y, 3D-view

5.3.1.14

L-Rhamnose = L-Rhamnulose

2631, 2624, 2627, 2635, 2636, 2637, 2629, 2632, 2633, 2634, 2626, 2630, 660751, 677350, 677768, 680947, 681406, 703677, 705332, 716819, 713643, 713898, 714530, 714573, 715213, 727230, 727653, 727537, 747355, 747394, 747820, 749202, 769709, 772450, 773107, 748497

4GJI, 3D-view

3.2.1.40

3 entries

5.3.1.14

8 entries

5.3.1.20

L-Rhamnose = L-Rhamnulose

2629, 2645, 2648

-

5.3.1.5

L-Rhamnose = ?

2735

-

5.3.1.6

L-Rhamnose = L-Rhamnulose

773509

-

Product in Enzyme-catalyzed Reactions (61 results)

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Show Product (61 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.247

beta-D-galactosyl-(1->4)-L-rhamnose + phosphate = L-rhamnose + alpha-D-galactose 1-phosphate

-

-

2.4.1.282

3-O-alpha-D-glucopyranosyl-L-rhamnopyranose + phosphate = L-rhamnose + beta-D-glucose 1-phosphate

-

-

3.2.1.172

2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 4-deoxy-alpha-L-threo-hex-4-enopyranuronate + L-rhamnopyranose

-

-

3.2.1.172

2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose

-

-

3.2.1.172

rhamnogalacturonan I + H2O = L-rhamnose + ?

-

-

3.2.1.174

rhamnogalacturonan I + H2O = L-rhamnose + ?

-

-

3.2.1.174

rhamnogalacturonan oligosaccharide + H2O = L-rhamnose + ?

-

-

3.2.1.172

3 entries

3.2.1.174

2 entries

3.2.1.188

4-nitrophenyl alpha-L-rhamnopyranoside + H2O = 4-nitrophenol + L-rhamnopyranose

-

-

3.2.1.189

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O = D-glucopyranose + 2 L-rhamnopyranose + diosgenin

-

-

3.2.1.189

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O = D-glucose + 2 L-rhamnose + diosgenin

-

-

3.2.1.189

polyphyllin VII + 4 H2O = 3 L-rhamnose + D-glucose + (22zeta,25R)-9zeta-spirost-5-en-3beta,17-diol

-

-

3.2.1.189

3-O-[alpha-L-Ara-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 3 H2O = D-glucopyranose + L-arabinose + L-rhamnopyranose + diosgenin

-

-

3.2.1.189

3-O-[alpha-L-Ara-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + H2O = D-glucose + L-rhamnose + L-arabinose + diosgenin

-

-

3.2.1.190

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 2 H2O = 2 L-rhamnopyranose + diosgenin 3-O-beta-D-glucopyranoside

-

-

3.2.1.190

3-O-[alpha-L-Rha-(1->4)-[alpha-L-Rha-(1->2)]-beta-D-Glc]diosgenin + 2 H2O = 2 L-rhamnopyranose + diosgenin-3-O-beta-D-glucopyranoside

-

-

3.2.1.189

5 entries

3.2.1.190

2 entries

3.2.1.192

ginsenoside Re + H2O = ginsenoside Rg2 + L-rhamnose

-

-

3.2.1.194

ginsenoside R1 + H2O = ginsenoside F1 + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside F1 + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside Rg1 + L-rhamnose

-

-

3.2.1.194

ginsenoside Re + H2O = ginsenoside Rg2 + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + 2 H2O = protopanaxatriol + D-glucose + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + H2O = ginsenoside Rh1 + L-rhamnose

-

-

3.2.1.194

ginsenoside Rg2 + H2O = protopanaxatriol + D-glucose + L-rhamnose

-

-

3.2.1.194

7 entries

3.2.1.195

ginsenoside Re + H2O = ginsenoside Rh1 + D-glucose + L-rhamnose

-

-

3.2.1.21

ginsenoside Re + H2O = ginsenoside Rg1 + L-rhamnose

-

-

3.2.1.21

ginsenoside Rg2 + H2O = ginsenoside Rh1 + L-rhamnose

-

-

3.2.1.21

2 entries

3.2.1.24

mannosyl rhamnose + H2O = alpha-D-mannopyranose + rhamnose

136025

-

3.2.1.40

4-nitrophenyl alpha-L-rhamnopyranoside + H2O = 4-nitrophenol + L-rhamnopyranose

-

-

3.2.1.40

4-nitrophenyl-alpha-L-rhamnopyranoside + H2O = 4-nitrophenol + L-rhamnopyranose

-

-

3.2.1.40

baohuoside I + H2O = icaritin + L-rhamnose

-

-

3.2.1.40

epimedin C + H2O = icariin + L-rhamnose

-

-

3.2.1.40

epoetin C + H2O = icariin + L-rhamnose

-

-

3.2.1.40

gellan + H2O = L-rhamnose + ?

-

-

3.2.1.40

hesperidin + H2O = ? + L-rhamnose

-

-

3.2.1.40

hesperidin + H2O = hesperetin 7-O-beta-D-glucoside + L-rhamnose

-

-

3.2.1.40

hesperidin + H2O = hesperetin-7-O-glucoside + L-rhamnose

-

-

3.2.1.40

hesperidin + H2O = L-rhamnose + ?

-

-

3.2.1.40

icariin + H2O = icarisid I + L-rhamnose

-

-

3.2.1.40

myricitrin + H2O = L-rhamnose + myricetin

136772

-

3.2.1.40

nairutin + H2O = ? + L-rhamnose

-

-

3.2.1.40

naringin + H2O = 4',5,7-trihydroxyflavanone 7-O-beta-D-glucoside + L-rhamnose

-

-

3.2.1.40

naringin + H2O = 4',5,7-trihydroxyflavanone-7-beta-D-glucoside + L-rhamnose

-

-

3.2.1.40

naringin + H2O = ? + L-rhamnose

-

-

3.2.1.40

naringin + H2O = L-rhamnose + ?

-

-

3.2.1.40

naringin + H2O = prunin + L-rhamnose

-

-

3.2.1.40

narirutin + H2O = ? + L-rhamnose

-

-

3.2.1.40

neohesperidin + H2O = hesperetin-7-O-glucoside + L-rhamnose

-

-

3.2.1.40

quercetin 3-alpha-L-rhamnopyranoside + H2O = quercetin + L-rhamnose

-

-

3.2.1.40

quercitrin + H2O = ? + L-rhamnose

-

-

3.2.1.40

quercitrin + H2O = quercetin + L-rhamnose

136772, -

-

3.2.1.40

rutin + H2O = ? + L-rhamnose

-

-

3.2.1.40

rutin + H2O = isoquercetin + L-rhamnose

-

-

3.2.1.40

rutin + H2O = isoquercitrin + L-rhamnose

-

-

3.2.1.40

rutin + H2O = L-rhamnose + ?

-

-

3.2.1.40

rutin + H2O = quercetin-3-beta-D-glucoside + L-rhamnose

-

-

3.2.1.40

rutinose + H2O = L-rhamnose + D-glucose

-

-

3.2.1.40

robinin + H2O = rhamnose + kaempferol-3-robinoside

136772

-

3.2.1.40

30 entries

3.2.1.43

O-beta-L-rhamnopyranosyl-(1-3)-O-beta-L-rhamnopyranosyl-(1-3)-L-rhamnose + H2O = L-rhamnose

136443

-

3.2.1.99

cell wall polysaccharide + H2O = arabinose + galactose + rhamnose + fucose

136937

-

3.2.1.B31

quercitrin + H2O = quercetin + L-rhamnose

-

-

5.3.1.14

L-rhamnulose = L-rhamnopyranose

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

4.2.2.24

5 mM, 1.24fold activation

707221

-

Inhibitor in Enzyme-catalyzed Reactions (14 results)

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Show Inhibitors (14 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.122

74% inhibition of L-glucose oxidation

285802

-

3.2.1.174

50% inhibition at 50 mM

753460

-

3.2.1.180

5 mM, 35% inhibition

709026

-

3.2.1.40

-

655015, 696898

-

3.2.1.40

10 mM, 14% residual activity; 10 mM, 37% residual activity

654359

-

3.2.1.40

compeitive

715802

-

3.2.1.40

competitive

654256, 654992, 656420, 656671

-

3.2.1.40

competitive inhibitor

768690

-

3.2.1.40

complete inhibition, competitive product inhibition; complete inhibition, competitive product inhibition

664775

-

3.2.1.40

crystallized complex with interacting site determined, for kinetic assay different concentrations ranging between 0 and 100 mM of rhamnose used

681462

-

3.2.1.40

isoform RhaB1 is slightly inhibited by L-rhamnose, showing noncompetitive inhibition

705564

-

3.2.1.40

product inhibition

775952

-

3.2.1.40

strong product inhibition

666000

-

3.2.1.40

10 entries

3.2.1.51

competitive inhibition, Ki: 140 mM

208720

-

3D Structure of Enzyme-Ligand-Complex (PDB) (7 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (7 entries)

EC NUMBER

ENZYME 3D STRUCTURE

5.3.1.14

1DE6, 3D-view

5.3.1.14

2I56, 3D-view

5.3.1.14

3ITT, 3D-view

5.3.1.14

3M0H, 3D-view

5.3.1.14

3M0V, 3D-view

5.3.1.14

3M0Y, 3D-view

5.3.1.14

4GJI, 3D-view

5.3.1.14

7 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (35 results)

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Show Turnover Number (35 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.173

1510

-

pH 9.0, 30°C, recombinant enzyme

687737

1.1.1.173

2860

-

pH 9.0, 30°C, recombinant enzyme

687737

1.1.1.173

2 entries

1.1.1.377

22.36

-

pH 7.0, 60°C

727435

1.1.1.378

11.35

-

recombinant mutant Q156A, pH 9.0, 30°C

763033

1.1.1.378

37.2

-

pH 9.0, 30°C, cosubstrate: NAD+

687737

1.1.1.378

38

-

recombinant mutant T191F, pH 9.0, 30°C

763033

1.1.1.378

55.5

-

recombinant mutant F99Y, pH 9.0, 30°C

763033

1.1.1.378

57

-

recombinant mutant F99A, pH 9.0, 30°C

763033

1.1.1.378

62.2

-

recombinant mutant D200H, pH 9.0, 30°C

763033

1.1.1.378

74.8

-

pH 9.0, 30°C, cosubstrate: NADP+

687737

1.1.1.378

80.3

-

recombinant mutant D200A, pH 9.0, 30°C

763033

1.1.1.378

83.5

-

recombinant wild-type enzyme, pH 9.0, 30°C

763033

1.1.1.378

137

-

recombinant mutant I196A, pH 9.0, 30°C

763033

2.4.1.247

50

-

recombinant enzyme, pH 7.0, 37°C, reverse reaction

722132

2.4.1.247

74

-

-

693235

1.1.1.378

10 entries

2.4.1.247

2 entries

2.4.1.282

1.6

-

pH 6.5, 30°C, reverse phosphorolysis reaction, cosubstrate beta-D-glucose 1-phosphate

714662

5.3.1.14

5.1

-

mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

7.7

-

pH 8.5, 60°C

747820

5.3.1.14

13.3

-

mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

50.5

-

in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C

714530

5.3.1.14

53.6

-

mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

68

-

pH 7.0, 65°C, recombinant enzyme

677768

5.3.1.14

99.9

-

in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C

727653

5.3.1.14

142

-

mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

146

-

purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)

714573

5.3.1.14

149.5

-

in 50 mM malate buffer, at pH 7.0 and 70°C

713898

5.3.1.14

153

-

pH 8.0, 60°C

747355

5.3.1.14

180

-

at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0

715213

5.3.1.14

192

-

mutant enzyme H101N, pH and temperature not specified in the publication

727537

5.3.1.14

195

-

at pH 8.0 and 75°C

727230

5.3.1.14

199.7

-

pH 7.0, 70°C, recombinant enzyme

748497

5.3.1.14

202.5

-

pH 7.0, 70°C, recombinant enzyme

747394

5.3.1.14

224

-

wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

374

-

wild type enzyme, pH and temperature not specified in the publication

727537

5.3.1.14

18 entries

5.3.1.6

129.4

-

pH 8.0, 50°C recombinant enzyme

773509

K_M Value (45 results)

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Show KM Value (45 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.173

0.2

-

-

347732, 347733

1.1.1.173

1.5

-

pH 8.0, 30°C, recombinant enzyme

686697

1.1.1.173

1.71

-

pH 9.0, 30°C, recombinant enzyme

687737

1.1.1.173

9.35

-

pH 9.0, 30°C, recombinant enzyme

687737

1.1.1.173

4 entries

1.1.1.21

52.3

-

-

286255

1.1.1.377

0.46

-

pH 7.0, 60°C

727435

1.1.1.378

2.23

-

recombinant wild-type enzyme, pH 9.0, 30°C

763033

1.1.1.378

2.34

-

pH 9.0, 30°C, cosubstrate: NADP+

687737

1.1.1.378

2.61

-

pH 9.0, 30°C, cosubstrate: NAD+

687737

1.1.1.378

7.73

-

recombinant mutant D200H, pH 9.0, 30°C

763033

1.1.1.378

11.3

-

recombinant mutant I196A, pH 9.0, 30°C

763033

1.1.1.378

13.7

-

recombinant mutant D200A, pH 9.0, 30°C

763033

1.1.1.378

26.1

-

recombinant mutant T191F, pH 9.0, 30°C

763033

1.1.1.378

37.9

-

recombinant mutant F99Y, pH 9.0, 30°C

763033

1.1.1.378

66.2

-

recombinant mutant F99A, pH 9.0, 30°C

763033

1.1.1.378

78.9

-

recombinant mutant Q156A, pH 9.0, 30°C

763033

2.4.1.247

2.3

-

recombinant enzyme, pH 7.0, 37°C, reverse reaction

722132

2.4.1.247

2.4

-

-

693235

1.1.1.378

10 entries

2.4.1.247

2 entries

2.4.1.282

2.7

-

pH 6.5, 30°C, reverse phosphorolysis reaction, cosubstrate beta-D-glucose 1-phosphate

714662

5.3.1.14

0.49

-

pH 8.5, 60°C

747820

5.3.1.14

0.7

-

-

2624, 2627

5.3.1.14

0.92

-

wild type enzyme, pH and temperature not specified in the publication

727537

5.3.1.14

1.03

-

in 50 mM potassium phosphate buffer (pH 7.0) and 1 mM Co2+, at 65°C

727653

5.3.1.14

1.36

-

pH 7.0, 70°C, recombinant enzyme

747394

5.3.1.14

2

-

-

2624, 2637

5.3.1.14

3.53

-

at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0

715213

5.3.1.14

3.54

-

pH 7.0, 70°C, recombinant enzyme

748497

5.3.1.14

4.89

-

pH 7.0, 65°C, recombinant enzyme

677768

5.3.1.14

5

-

in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C

714530

5.3.1.14

7.9

-

mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

9.4

-

mutant enzyme H101N, pH and temperature not specified in the publication

727537

5.3.1.14

11.9

-

50°C, pH 9.0, recombinant enzyme

660751

5.3.1.14

12.2

-

mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

18.5

-

mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

19.4

-

wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

24.2

-

mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C

716819

5.3.1.14

24.6

-

at pH 8.0 and 75°C

727230

5.3.1.14

33.8

-

pH 7.5, 65°C

749202

5.3.1.14

37

-

purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)

714573

5.3.1.14

53

-

pH 8.0, 60°C

747355

5.3.1.14

55

-

-

2633

5.3.1.14

55

-

50°C, pH 9.0, intrinsic enzyme from Pseudomonas stutzeri

660751

5.3.1.14

528

-

in 50 mM malate buffer, at pH 7.0 and 70°C

713898

5.3.1.14

24 entries

5.3.1.5

312

-

-

2735

5.3.1.6

43.47

-

pH 8.0, 50°C recombinant enzyme

773509

K_i Value (16 results)

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Show KI Value (16 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.40

1.28

-

pH 7.5, 50°C, recombinant RhmA, versus 4-nitrophenyl alpha-L-rhamnopyranoside

664775

3.2.1.40

1.4

6.5

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

1.5

-

pH 4.5, 30°C

654256

3.2.1.40

1.8

-

crystallized complex with interacting site analyzed

681462

3.2.1.40

2

5

pH 6.5, 30°C

654992

3.2.1.40

2.1

-

pH 5.5, 40°C

655015

3.2.1.40

2.37

-

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

2.5

-

-

656420

3.2.1.40

2.5

-

pH 5.0, 37°C, versus 4-nitrophenyl alpha-L-rhamnopyranoside

768690

3.2.1.40

2.56

4.94

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

4.2

-

pH 4.5, 30°C

654256

3.2.1.40

4.2

-

pH 5.0, 37°C, versus naringin

768690

3.2.1.40

4.65

-

pH 7.0, 50°C, recombinant RhmB, versus 4-nitrophenyl alpha-L-rhamnopyranoside

664775

3.2.1.40

4.7

-

pH 9.5, 37°C

715802

3.2.1.40

19.88

-

isoform RhaB1

705564

3.2.1.40

15 entries

3.2.1.51

140

-

competitive inhibition

208720

IC₅₀ Value (4 results)

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Show IC50 Value (4 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.2.1.40

4.9

-

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

5.5

-

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

8.3

-

recombinant wild-type enzyme, pH 7.0, 80°C

775952

3.2.1.40

20

-

pH 7.8, 40°C

696898

3.2.1.40

4 entries

References & Links

Literature References (97)

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Show Reference (97 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2624

-

Aldose-ketose isomerases

1972

Noltmann, E.A.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

6

271-354

2626

-

Ueber den Abbau der Desoxyzucker durch Bacterienenzyme. I. L-Rhamnose-isomerase aus Lactobacillus plantarum

1963

Domagk, G.F.; Zech, R.

Biochem. Z.

339

145-153

2627

-

L-Rhamnose isomerase

1966

Domagk, G.F.; Zech, R.

Methods Enzymol.

9

579-582

2629

1262310

Evidence that the isomerization of D-ribose and L-rhamnose is catalyzed by the same enzyme in Mycobacterium smegmatis

1976

Izumori, K.; Mitchell, M.; Elbein, A.D.

J. Bacteriol.

126

553-555

2630

182906

Metabolism of L-rhamnose in Arthrobacter pyridinolis

1976

Levinson, S.L.; Krulwich, T.A.

J. Gen. Microbiol.

95

277-286

2631

6373710

L-Rhamnose utilization in Salmonella typhimurium

1984

Akhy, M.T.; Brown, C.M.; Old, D.C.

J. Appl. Bacteriol.

56

269-274

2632

-

Immobilization of L-rhamnose isomerase and its application in L-mannose production from L-fructose

1997

Bhuiyan, S.H.; Itami, Y.; Izumori, K.

J. Ferment. Bioeng.

84

558-562

2633

-

Isolation of an L-rhamnose isomerase-constitutive mutant of Pseudomonas sp. strain LL172: purification and characterization of the enzyme

1997

Bhuiyan, S.H.; Itami, Y.; Izumori, K.

J. Ferment. Bioeng.

84

319-323

2634

-

D-Allose production from D-psicose using immobilized D-rhamnose isomerase

1998

Bhuiyan, S.H.; Itami, Y.; Rokui, Y.; Katayama, T.; Izumori, K.

J. Ferment. Bioeng.

85

539-541

2635

8564401

Cloning and overexpression of rhamnose isomerase and fucose isomerase

1995

Garcia-Junceda, E.; Shen, G.J.; Alajarin, R.; Wong, C.H.

Bioorg. Med. Chem.

3

1349-1355

2636

2558952

Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12

1989

Badia, J.; Baldoma, L.; Aguilar, J.; Boronat, A.

FEMS Microbiol. Lett.

65

253-258

2637

1650346

L-Lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose

1991

Badia, J.; Gimenez, R.; Baldoma, L.; Barnes, E.; Fessner, W.D.; Aguilar, J.

J. Bacteriol.

173

5144-5150

2645

240851

Purification, crystallization, and properties of D-ribose isomerase from Mycobacterium smegmatis

1975

Izumori, K.; Rees, A.W.; Elbein, A.D.

J. Biol. Chem.

250

8085-8087

2648

7144588

D-Ribose isomerase

1982

Elbein, A.D.; Izumori, K.

Methods Enzymol.

89

547-550

2735

239628

Properties of D-xylose isomerase from Streptomyces albus

1975

Sanchez, S.; Smiley, K.L.

Appl. Microbiol.

29

745-750

136025

4968617

alpha-Mannosidase and beta-mannosidase from the liver of Turbo cortunus: Purification, properties and application in carbohydrate research

1967

Muramatsu, T.; Egami, F.

J. Biochem.

62

700-709

136443

-

Arrangement of the L-rhamnose units in Diplococcus pneumoniae type II polysaccharide

1965

Barker, S.A.; Somers, P.J.; Stacey, M.

Carbohydr. Res.

1

106-115

136772

-

Microbial degradation of quercitrin

1963

Westlake, D.W.S.

Can. J. Microbiol.

9

211-220

136937

-

Hemi-cellulases in enzymic fruit processing

1982

Voragen, A.G.J.; Geerst, F.; Pilnik, W.

Util. Enzymes Technol. Aliment. , Symp. Int. (Dupuy, P. , ed. ), Tech. Doc. Lavoisier Paris

-

497-502

171351

-

Purification, properties and characterization of a high-molecular-mass beta-galactosidase isoenzyme from Thermus aquaticus

1997

Berger, J.L.; Lee, B.H.; Lacroix, C.

Biotechnol. Appl. Biochem.

25

29-41

208720

7317440

Porcine thyroid fucosidase

1981

Grove, D.S.; Serif, G.S.

Biochim. Biophys. Acta

662

246-255

285802

40609

Oxidation of L-glucose by a pseudomonad

1979

Sasajima, K.I.; Sinskey, A.J.

Biochim. Biophys. Acta

571

120-126

285901

-

Characterization of D-sorbitol dehydrogenase involved in D-sorbitol production of a methanol yeast, Candida boidinii (Kloeckera sp.) No. 2201

1988

Vongsuvanlert, V.; Tani, Y.

Agric. Biol. Chem.

52

419-426

286118

9168914

The stereospecificity of hydrogen transfer to NAD(P)+ catalyzed by lactol dehydrogenases

1997

Mostad, S.B.; Helming, H.L.; Groom, C.; Glasfeld, A.

Biochem. Biophys. Res. Commun.

233

681-686

286255

12223702

Characterization and purification of an aldose from the acidophilic and thermophilic red algae Galdiera sulphuraria

1997

Gross, W.; Seipold, P.; Schnarrenberger, C.

Plant Physiol.

114

231-236

347732

-

The application of immobilized alpha-L-rhamnosidase and L-rhamnosedehydrogenase in the analysis of L-rhamnose and alpha-L-rhamnosides

1987

Pittner, F.; Turecek, P.L.

Appl. Biochem. Biotechnol.

16

15-24

347733

8142

L-Rhamnose dehydrogenase of pullularia pullulans

1976

Rigo, L.U.; Nakano, M.; Veiga, L.A.; Feingold, D.S.

Biochim. Biophys. Acta

445

286-293

347736

-

L-Rhamnose metabolism in Pichia stipitis and Debaryomyces polymorphus

1994

Twerdochlib, A.L.; Pedrosa, F.O.; Funayama, S.; Rigo, L.U.

Can. J. Microbiol.

40

896-902

348276

-

Gluconsäure bildende Enzyme bei Aspergillus niger

1980

Matsushita, K.; Ohno, Y.; Shinagawa, E.; Adachi, O.; Ameyama, M.

Agric. Biol. Chem.

44

1505-1512

488677

-

Trihalo-trideoxy galactosucrose compounds

1985

Rathbone, E.B.; Hacking, A.J.; Cheetham, P.S.J.

UK Patent Application

GB21

45080 A

639191

3800975

Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41

1986

Dokter, P.; Frank, J.; Duine, J.A.

Biochem. J.

239

163-167

639203

-

L-Glucose dehydrogenase of Gluconobacter suboxydans: solubilization, purification and characterization

1981

Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.

Agric. Biol. Chem.

45

851-861

641670

5646161

The metabolism of L-fucose. 3. The enzymatic synthesis of beta-L-fucose 1-phosphate

1968

Ishihara, H.; Massaro, D.J.; Heath, E.C.

J. Biol. Chem.

243

1103-1109

654256

11319105

Purification and characterization of two different alpha-L-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus

2001

Manzanares, P.; van den Broeck, H.C.; de Graaff, L.H.; Visser, J.

Appl. Environ. Microbiol.

67

2230-2234

654359

12831847

Molecular identification of an alpha-L-rhamnosidase from Bacillus sp strain GL1 as an enzyme involved in complete metabolism of gellan

2003

Hashimoto, W.; Miyake, O.; Nankai, H.; Murata, K.

Arch. Biochem. Biophys.

415

235-244

654992

11129592

Purification and characterization of an alpha-L-rhamnosidase from Pichia angusta X349

2000

Yanai, T.; Sato, M.

Biosci. Biotechnol. Biochem.

64

2179-2185

655015

12224626

Thermal inactivation and product inhibition of Aspergillus terreus CECT 2663 alpha-L-rhamnosidase and their role on hydrolysis of naringin solutions

2002

Soria, F.; Ellenrieder, G.

Biosci. Biotechnol. Biochem.

66

1442-1449

656420

-

Purification and characterization of an a-L-rhamnosidase from Aspergillus terreus of interest in winemaking

2001

Gallego, M.V.; Pinaga, F.; Ramon, D.; Valles, S.

J. Food Sci.

66

204-209

656671

10972728

Purification and characterization of an alpha-L-rhamnosidase from Aspergillus nidulans

2000

Manzanares, P.; Orejas, M.; Ibanez, E.; Valles, S.; Ramon, D.

Lett. Appl. Microbiol.

31

198-202

660751

15184124

Cloning, nucleotide sequence, and overexpression of the L-rhamnose isomerase gene from Pseudomonas stutzeri in Escherichia coli

2004

Leang, K.; Takada, G.; Ishimura, A.; Okita, M.; Izumori, K.

Appl. Environ. Microbiol.

70

3298-3304

664775

-

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Links to other databases for L-rhamnopyranose

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