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BKMS-react is an integrated and non-redundant biochemical reaction database containing known enzyme-catalyzed and spontaneous reactions. Biochemical reactions collected from BRENDA, KEGG, MetaCyc and SABIO-RK were matched and integrated by aligning substrates and products.
 

:= BRENDA, := KEGG, := MetaCyc, := SABIO-RK
:= amino acid sequences := show the reaction diagram
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  • EC Number
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Results 1 - 10 of 124
EC Number
Reaction
Pathways
Reaction IDs
Stoichiometry Check  
Commentary
inositol-hexakisphosphate kinase
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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: This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to Ins(PP)P(4), isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P(4) and Ins(1,2,3,4,6)P(5) at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP(6)), respectively. Yeast produce InsP(6) from Ins(1,4,5)P(3) by the actions of this enzyme and EC 2.7.1.158.
inositol-tetrakisphosphate 1-kinase
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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: This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to Ins(PP)P(4), isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P(4) and Ins(1,2,3,4,6)P(5) at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP(6)), respectively. Yeast produce InsP(6) from Ins(1,4,5)P(3) by the actions of this enzyme and EC 2.7.1.158.
inositol-polyphosphate multikinase
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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: This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to Ins(PP)P(4), isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P(4) and Ins(1,2,3,4,6)P(5) at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP(6)), respectively. Yeast produce InsP(6) from Ins(1,4,5)P(3) by the actions of this enzyme and EC 2.7.1.158.
inositol-1,3,4-trisphosphate 5/6-kinase
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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: This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to Ins(PP)P(4), isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P(4) and Ins(1,2,3,4,6)P(5) at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP(6)), respectively. Yeast produce InsP(6) from Ins(1,4,5)P(3) by the actions of this enzyme and EC 2.7.1.158.
Diaminopropionate ammonia-lyase
2,3-diaminopropanoate + H2O = pyruvate + 2 NH3
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mugineic-acid 3-dioxygenase
mugineic acid + 2-oxoglutarate + O2 = 3-epihydroxymugineic acid + succinate + CO2
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mugineic-acid 3-dioxygenase
2'-deoxymugineic acid + 2-oxoglutarate + O2 = 3-epihydroxy-2'-deoxymugineic acid + succinate + CO2
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zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
generic compounds
: zeaxanthin epoxidase first step of two-step reaction (see R10070, R06946+R06947)
: A flavoprotein (FAD) that is active under conditions of low light. Along with EC 1.10.99.3, violaxanthin de-epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. It will also epoxidize lutein in some higher-plant species.
zeaxanthin epoxidase
zeaxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = antheraxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
generic compounds
: zeaxanthin epoxidase first step of two-step reaction (see R10070, R06946+R06947)
: A flavoprotein (FAD) that is active under conditions of low light. Along with EC 1.10.99.3, violaxanthin de-epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle, which is involved in protecting the plant against damage by excess light. It will also epoxidize lutein in some higher-plant species.
Results 1 - 10 of 124