Glutinol synthase

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Glutinol synthase
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EC no. 5.4.99.49
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Glutinol synthase (EC 5.4.99.49) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, glutinol-forming). [1] This enzyme catalyses the following chemical reaction

(3S)-2,3-epoxy-2,3-dihydrosqualene glutinol

The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids.

Related Research Articles

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α-Amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

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Parkeol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Achilleol B synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Friedelin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

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α-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Marneral synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase. This enzyme catalyses the following chemical reaction

β-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

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Tirucalladienol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Baruol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

References

  1. Wang Z, Yeats T, Han H, Jetter R (September 2010). "Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids". The Journal of Biological Chemistry. 285 (39): 29703–12. doi: 10.1074/jbc.m109.098871 . PMC   2943309 . PMID   20610397.