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EC
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1.14.13.87
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| Transferred entry: | licodione synthase. Now EC 1.14.14.140, licodione synthase
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| [EC 1.14.13.87 created 2004, deleted 2018] |
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EC
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1.14.14.140
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| Transferred entry: | licodione synthase. Now included with EC 1.14.14.162, flavanone 2-hydroxylase
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| [EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162, deleted 2018] |
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| EC |
1.14.14.162 |
| Accepted name: |
flavanone 2-hydroxylase |
| Reaction: |
a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 2-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of licodione biosynthesis, click here |
| Other name(s): |
CYP93G2 (gene name); CYP93B1 (gene name); (2S)-flavanone 2-hydroxylase; licodione synthase |
| Systematic name: |
flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating) |
| Comments: |
A cytochrome P-450 (heme thiolate) plant enzyme that catalyses the 2-hydroxylation of multiple flavanones such as (2S)-naringenin, (2S)-eriodictyol, (2S)-pinocembrin, and (2S)-liquiritigenin. The products are meta-stable and exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Otani, K., Takahashi, T., Furuya, T. and Ayabe, S. Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol. 105 (1994) 1427–1432. [PMID: 12232298] |
| 2. |
Akashi, T., Aoki, T. and Ayabe, S. Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431 (1998) 287–290. [DOI] [PMID: 9708921] |
| 3. |
Du, Y., Chu, H., Chu, I.K. and Lo, C. CYP93G2 is a flavanone 2-hydroxylase required for C-glycosylflavone biosynthesis in rice. Plant Physiol. 154 (2010) 324–333. [PMID: 20647377] |
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| [EC 1.14.14.162 created 2018. EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162] |
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| EC |
2.1.1.65 |
| Accepted name: |
licodione 2′-O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + 2′-O-methyllicodione |
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For diagram of licodione biosynthesis, click here |
| Systematic name: |
S-adenosyl-L-methionine:licodione 2′-O-methyltransferase |
| Comments: |
As well as licodione [1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)-1,3-propanedione], the 2′′-hydroxy-derivative and isoliquiritigenin can act as acceptors, but more slowly. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 77000-07-8 |
| References: |
| 1. |
Ayabe, S.-I., Yoshikawa, T., Kobayashi, M. and Furuya, T. Biosynthesis of retrochalcone, echinatin: involvement of O-methyltransferase to licodione. Phytochemistry 19 (1980) 2331–2336. |
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| [EC 2.1.1.65 created 1983] |
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| EC |
2.1.1.154 |
| Accepted name: |
isoliquiritigenin 2′-O-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2′-O-methylisoliquiritigenin |
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For diagram of daidzein biosynthesis, click here |
| Glossary: |
isoliquiritigenin = 4,2′,4′-trihydroxychalcone |
| Other name(s): |
chalcone OMT; CHMT |
| Systematic name: |
S-adenosyl-L-methionine:isoliquiritigenin 2′-O-methyltransferase |
| Comments: |
Not identical to EC 2.1.1.65, licodione 2′-O-methyltransferase [2]. While EC 2.1.1.154, isoliquiritigenin 2′-O-methyltransferase can use licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin as a substrate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 139317-14-9 |
| References: |
| 1. |
Maxwell, C.A., Edwards, R. and Dixon, R.A. Identification, purification, and characterization of S-adenosyl-L-methionine: isoliquiritigenin 2′-O-methyltransferase from alfalfa (Medicago sativa L.). Arch. Biochem. Biophys. 293 (1992) 158–166. [DOI] [PMID: 1731632] |
| 2. |
Ichimura, M., Furuno, T., Takahashi, T., Dixon, R.A. and Ayabe, S. Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa and licorice cultures. Phytochemistry 44 (1997) 991–995. [DOI] [PMID: 9055445] |
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| [EC 2.1.1.154 created 2004] |
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