EC |
1.1.1.349 |
Accepted name: |
norsolorinic acid ketoreductase |
Reaction: |
(1′S)-averantin + NADP+ = norsolorinic acid + NADPH + H+ |
Glossary: |
norsolorinic acid = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone
(1′S)-averantin = 1,3,6,8-tetrahydroxy-[(1S)-2-hydroxyhexyl]-9,10-anthraquinone |
Other name(s): |
aflD (gene name); nor-1 (gene name) |
Systematic name: |
(1′S)-averantin:NADP+ oxidoreductase |
Comments: |
Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486–2492. [PMID: 8368836] |
2. |
Zhou, R. and Linz, J.E. Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 65 (1999) 5639–5641. [PMID: 10584035] |
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[EC 1.1.1.349 created 2013] |
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EC |
1.13.12.20 |
Accepted name: |
noranthrone monooxygenase |
Reaction: |
norsolorinic acid anthrone + O2 = norsolorinic acid + H2O |
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For diagram of aflatoxin biosynthesis (part 1), click here |
Glossary: |
norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
norsolorinate = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone |
Other name(s): |
norsolorinate anthrone oxidase |
Systematic name: |
norsolorinic acid anthrone:oxygen 9-oxidoreductase (norsolorinic acid-forming) |
Comments: |
Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ehrlich, K.C., Li, P., Scharfenstein, L. and Chang, P.K. HypC, the anthrone oxidase involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 76 (2010) 3374–3377. [DOI] [PMID: 20348292] |
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[EC 1.13.12.20 created 2013] |
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EC
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1.14.13.174
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Transferred entry: | averantin hydroxylase. Now EC 1.14.14.116, averantin hydroxylase
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[EC 1.14.13.174 created 2013, deleted 2018] |
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EC |
1.14.14.116 |
Accepted name: |
averantin hydroxylase |
Reaction: |
(1) (1′S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1′S,5′S)-5′-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O (2) (1′S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1′S,5′R)-5′-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O
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For diagram of aflatoxin biosynthesis (part 1), click here |
Glossary: |
averantin = 1,3,6,8-tetrahydroxy-2-[(1S)-1-hydroxyhexyl]anthracene-9,10-dione
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Other name(s): |
AVN hydroxylase; avnA (gene name); CYP60A1 |
Systematic name: |
(1′S)-averantin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5′-hydroxylating) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein isolated from the saprophytic mold Aspergillus parasiticus. Involved in aflatoxin biosynthesis. Does not react with (1′R)-averantin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486–2492. [PMID: 8368836] |
2. |
Yu, J., Chang, P.K., Cary, J.W., Bhatnagar, D. and Cleveland, T.E. avnA, a gene encoding a cytochrome P-450 monooxygenase, is involved in the conversion of averantin to averufin in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 63 (1997) 1349–1356. [PMID: 9097431] |
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[EC 1.14.14.116 created 2013 as EC 1.14.13.174, transferred 2018 to EC 1.14.14.116] |
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EC |
2.3.1.221 |
Accepted name: |
noranthrone synthase |
Reaction: |
7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O |
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For diagram of polyketides biosynthesis, click here |
Glossary: |
norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one |
Other name(s): |
polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase |
Systematic name: |
malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming) |
Comments: |
A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243–246. [DOI] [PMID: 18403714] |
2. |
Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139–1143. [DOI] [PMID: 19847268] |
3. |
Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246–6251. [DOI] [PMID: 20332208] |
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[EC 2.3.1.221 created 2013] |
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