BRENDA - Enzyme Database show
show all sequences of 1.14.14.102

Digital gene expression analysis provides insight into the transcript profile of the genes involved in aporphine alkaloid biosynthesis in lotus (Nelumbo nucifera)

Yang, M.; Zhu, L.; Li, L.; Li, J.; Xu, L.; Fen, J.; Liu, Y.; Front. Plant Sci. 8, 80 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene LOC104585940 encoding isozyme 2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
Nelumbo nucifera
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
Nelumbo nucifera
-
(S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Nelumbo nucifera
A0A1U7Z269
isozyme 2; 2 isozymes, 2 cultivars
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Nelumbo nucifera
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
745008
Nelumbo nucifera
(S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P-450
-
Nelumbo nucifera
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
Nelumbo nucifera
Cloned(Commentary) (protein specific)
Commentary
Organism
gene LOC104585940 encoding isozyme 2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
Nelumbo nucifera
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P-450
-
Nelumbo nucifera
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
Nelumbo nucifera
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
Nelumbo nucifera
-
(S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Nelumbo nucifera
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2
-
745008
Nelumbo nucifera
(S)-3'-hydroxy-N-methylcoclaurine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the common pathway of benzylisoquinoline alkaloid biosynthesis and the aporphine alkaloid bisynthesis pathway in lotus, overview. A series of enzymes, norcoclaurine 6-O-methyltransferase (6OMT), coclaurineN-methyltransferase (CNMT), (S)-N-methylcoclaurine-3-hydroxylase (NMCH), and 3-hydroxy-N-methylcoclaurine 4'-O-methyltransferase(4'OMT), exhibit catalytic activity to yield the central branchpoint intermediate (S)-reticuline
Nelumbo nucifera
physiological function
the expression of isozyme 1 is low in the two cultivars, so it may have little effect on alkaloid contents. The expression of CYP80B, NNU08355, has a positive effect on aporphine alkaloids content in lotus, but exhibits phenotypic lag, which might be because of NMCH which acts early in the benzylisoquinoline alkaloid biosynthetic pathway
Nelumbo nucifera
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the common pathway of benzylisoquinoline alkaloid biosynthesis and the aporphine alkaloid bisynthesis pathway in lotus, overview. A series of enzymes, norcoclaurine 6-O-methyltransferase (6OMT), coclaurineN-methyltransferase (CNMT), (S)-N-methylcoclaurine-3-hydroxylase (NMCH), and 3-hydroxy-N-methylcoclaurine 4'-O-methyltransferase(4'OMT), exhibit catalytic activity to yield the central branchpoint intermediate (S)-reticuline
Nelumbo nucifera
physiological function
the expression of isozyme 1 is low in the two cultivars, so it may have little effect on alkaloid contents. The expression of CYP80B, NNU08355, has a positive effect on aporphine alkaloids content in lotus, but exhibits phenotypic lag, which might be because of NMCH which acts early in the benzylisoquinoline alkaloid biosynthetic pathway
Nelumbo nucifera
Other publictions for EC 1.14.14.102
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745008
Yang
Digital gene expression analy ...
Nelumbo nucifera
Front. Plant Sci.
8
80
2017
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2
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720710
Desgagne-Penix
Systematic silencing of benzyl ...
Papaver somniferum
Plant J.
72
331-344
2012
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1
1
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687887
Cho
Synergistic effects of sequent ...
Eschscholzia californica
J. Biotechnol.
135
117-122
2008
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701436
Zhou
-
Molecular cloning and sequence ...
Coptis chinensis
Zhong Cao Yao
39
419-423
2008
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1
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1
1
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688821
Frick
Metabolic engineering with a m ...
Papaver somniferum
Metab. Eng.
9
169-176
2007
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1
1
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670561
Samanani
The role of phloem sieve eleme ...
Papaver somniferum
Plant J.
47
547-563
2006
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660256
Alcantara
Sanguinarine biosynthesis is a ...
Papaver somniferum
Plant Physiol.
138
173-183
2005
1
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1
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660086
Huang
Distribution of morphinan and ...
Papaver bracteatum, Papaver orientale, Papaver rhoeas, Papaver somniferum
Phytochemistry
53
555-564
2000
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285356
Pauli
Molecular cloning and function ...
Eschscholzia californica
Plant J.
13
793-801
1998
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5
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