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IUBMB Comments The enzyme is involved in the biosynthesis of aklaviketone, an intermediate in the biosynthetic pathways leading to formation of several anthracycline antibiotics, including aclacinomycin, daunorubicin and doxorubicin.
5.5.1.23
desaturase
arachidonic
delta6-desaturase
polyunsaturated
delta5
alpha-linolenic
b5-like
histidine-rich
di-homo-gamma-linolenic
daunomycin
desaturation
alpina
oleic
delta5-desaturation
polyketide
mortierella
Synonyms
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methyl aklanonate cyclase
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AcmA
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AknH
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aklaviketone = methyl aklanonate
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MetaCyc
aclacinomycin biosynthesis, daunorubicin biosynthesis
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aklaviketone lyase (decyclizing)
The enzyme is involved in the biosynthesis of aklaviketone, an intermediate in the biosynthetic pathways leading to formation of several anthracycline antibiotics, including aclacinomycin, daunorubicin and doxorubicin.
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methyl aklanonate
aklaviketone
methyl aklanonate
aklaviketone
Substrates: -
?
methyl aklanonate
aklaviketone
Substrates: -
?
methyl aklanonate
aklaviketone
-
Substrates: -
?
methyl aklanonate
aklaviketone
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Substrates: base-catalyzed mechanism
?
methyl aklanonate
aklaviketone
Substrates: the enzyme is involved in the biosynthesis of the anthracycline daunorubicin
?
methyl aklanonate
aklaviketone
Substrates: -
?
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methyl aklanonate
aklaviketone
methyl aklanonate
aklaviketone
Substrates: -
?
methyl aklanonate
aklaviketone
Substrates: -
?
methyl aklanonate
aklaviketone
-
Substrates: -
?
methyl aklanonate
aklaviketone
Substrates: the enzyme is involved in the biosynthesis of the anthracycline daunorubicin
?
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additional information
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enzyme activity is not accelerated or significantly inhibited by divalent metal ions (Zn2+, Co2+, Fe2+, Cu2+, or Mn2+) or chelating reagents
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additional information
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enzyme activity is not accelerated or significantly inhibited by divalent metal ions (Zn2+, Co2+, Fe2+, Cu2+, or Mn2+) or chelating reagents
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0.0521
methyl aklanonate
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pH 7.0, 30°C
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6 - 7.5
AAME cyclase activity is observed at both pH 7.5 and pH 6.0, suggesting that it has a broad optimal pH range for activity
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6.5 - 9
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pH 6.5: about 65% of maximal activity, 9.0: about 30% of maximal activity
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UniProt
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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physiological function
the enzyme is involved in the biosynthesis of the anthracycline daunorubicin
physiological function
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the enzyme is involved in biosynthesis of aklaviketone, an intermediate in the biosynthetic pathway to daunorubicin and doxorubicin
physiological function
enzyme is part of the akn gene cluster needed for aklavinone biosynthesis. It is responsible for closing the last ring of the aclacinomycin aglycone moiety
physiological function
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enzyme is part of the akn gene cluster needed for aklavinone biosynthesis. It is responsible for closing the last ring of the aclacinomycin aglycone moiety
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DNRD_STRGJ
144
0
16731
Swiss-Prot
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DNRD_STRPE
145
0
16701
Swiss-Prot
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DNRD_STRS5
161
0
18495
Swiss-Prot
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16000
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x * 16000, SDS-PAGE
16572
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x * 16572, electrospray MS analysis
18495
x * 18495, calculated from sequence
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?
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x * 16000, SDS-PAGE
?
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x * 16572, electrospray MS analysis
?
x * 18495, calculated from sequence
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overexpressed in Escherichia coli
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Kendrew, S.G.; Katayama, K.; Deutsch, E.; Madduri, K.; Hutchinson, C.R.
DnrD cyclase involved in the biosynthesis of doxorubicin: purification and characterization of the recombinant enzyme
Biochemistry
38
4794-4799
1999
Streptomyces peucetius
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Dickens, M.L.; Ye, J.; Strohl, W.R.
Analysis of clustered genes encoding both early and late steps in daunomycin biosynthesis by Streptomyces sp. strain C5
J. Bacteriol.
177
536-543
1995
Streptomyces sp. (Q55215)
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Rty, K.; Kantola, J.; Hautala, A.; Hakala, J.; Ylihonko, K.; Mntsl, P.
Cloning and characterization of Streptomyces galilaeus aclacinomycins polyketide synthase (PKS) cluster
Gene
293
115-122
2002
Streptomyces galilaeus (O52646), Streptomyces galilaeus, Streptomyces galilaeus ATCC 31615 (O52646)
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