EC Number |
Natural Substrates |
---|
1.14.15.24 | alpha-carotene + reduced acceptor + H+ + O2 |
- |
1.14.15.24 | beta-carotene + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
- |
1.14.15.24 | beta-carotene + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
the enzyme prefers alpha-carotene over beta-carotene as a substrate |
1.14.15.24 | beta-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2 |
- |
1.14.15.24 | beta-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2 |
the enzyme from the yeast Xanthophyllomyces dendrorhous is bifunctional and also catalyses the activity of beta-carotene 4-ketolase |
1.14.15.24 | beta-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2 |
the enzyme plays an important role in astaxanthin production |
1.14.15.24 | beta-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
- |
1.14.15.24 | beta-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
LUT1/CYP97C1 protein reveals a major beta-carotene hydroxylase activity in vivo when depleted in its preferred substrate alpha-carotene |
1.14.15.24 | beta-carotene + reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
the enzyme can convert not only the (un-substituted) beta ring but also the 4-ketolated beta-ring into the respective 3-hydroxylated groups |
1.14.15.24 | beta-carotene + reduced ferredoxin [iron-sulfur] cluster + H+ + O2 |
- |