N-methylcoclaurine 3'-monooxygenase

Last updated
N-methylcoclaurine 3'-monooxygenase
Identifiers
EC no. 1.14.13.71
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a N-methylcoclaurine 3'-monooxygenase (EC 1.14.13.71) is an enzyme that catalyzes the chemical reaction

(S)-N-methylcoclaurine + NADPH + H+ + O2 (S)-3'-hydroxy-N-methylcoclaurine + NADP+ + H2O

The 4 substrates of this enzyme are (S)-N-methylcoclaurine, NADPH, H+, and O2, whereas its 3 products are (S)-3'-hydroxy-N-methylcoclaurine, NADP+, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (3'-hydroxylating). This enzyme is also called N-methylcoclaurine 3'-hydroxylase and CYP80B1. [1]

Related Research Articles

In enzymology, a 2,4-dichlorophenol 6-monooxygenase (EC 1.14.13.20) is an enzyme that catalyzes the chemical reaction

In enzymology, a 24-hydroxycholesterol 7alpha-hydroxylase (EC 1.14.13.99) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3,9-dihydroxypterocarpan 6a-monooxygenase (EC 1.14.13.28) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-hydroxyphenylacetate 6-hydroxylase (EC 1.14.13.63) is an enzyme that catalyzes the chemical reaction

In enzymology, a 4'-methoxyisoflavone 2'-hydroxylase (EC 1.14.14.89, Formerly EC 1.14.13.53) is an enzyme that catalyzes the chemical reaction

7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase (EC 1.14.14.139, previously EC 1.14.13.95) is an enzyme that catalyzes the chemical reaction:

In enzymology, a (+)-abscisic acid 8'-hydroxylase (EC 1.14.13.93) is an enzyme that catalyzes the chemical reaction

In enzymology, a benzoate 4-monooxygenase (EC 1.14.14.92, Formerly EC 1.14.13.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a benzoyl-CoA 3-monooxygenase (EC 1.14.13.58) is an enzyme that catalyzes the chemical reaction:

In enzymology, a berbamunine synthase (EC 1.14.19.66, Formerly EC 1.1.3.34 and EC 1.14.21.3) is an enzyme that catalyzes the chemical reaction

In enzymology, a cholesterol 7alpha-monooxygenase (EC 1.14.13.17) is an enzyme that catalyzes the chemical reaction

In enzymology, a deoxysarpagine hydroxylase (EC 1.14.13.91) is an enzyme that catalyzes the chemical reaction

In enzymology, a flavonoid 3'-monooxygenase (EC 1.14.14.82, was wrongly classified as EC 1.14.13.21 in the past) is an enzyme that catalyzes the chemical reaction

In enzymology, an isoflavone 2'-hydroxylase (EC 1.14.14.90, Formerly EC 1.14.13.89) is an enzyme that catalyzes the chemical reaction

In enzymology, an isoflavone 3'-hydroxylase (EC 1.14.14.88, Formerly EC 1.14.13.52) is an enzyme that catalyzes the chemical reaction

In enzymology, a leukotriene-E4 20-monooxygenase (EC 1.14.13.34) is an enzyme that catalyzes the chemical reaction

In enzymology, a lithocholate 6beta-hydroxylase (EC 1.14.13.94) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">L-lysine 6-monooxygenase (NADPH)</span> Class of enzymes

In enzymology, a L-lysine 6-monooxygenase (NADPH) (EC 1.14.13.59) is an enzyme that catalyzes the chemical reaction

In enzymology, a methyltetrahydroprotoberberine 14-monooxygenase (EC 1.14.13.37) is an enzyme that catalyzes the chemical reaction

In enzymology, a (S)-limonene 3-monooxygenase (EC 1.14.13.47) is an enzyme that catalyzes the chemical reaction

References

  1. Pauli HH, Kutchan TM (1998). "Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3'-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent mono-oxygenase of benzylisoquinoline alkaloid biosynthesis". Plant J. 13 (6): 793–801. doi:10.1046/j.1365-313X.1998.00085.x. PMID   9681018.