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Information on EC 1.14.13.180 - aklavinone 12-hydroxylase and Organism(s) Streptomyces purpurascens and UniProt Accession Q54530

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IUBMB Comments
The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase.
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This record set is specific for:
Streptomyces purpurascens
UNIPROT: Q54530
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The taxonomic range for the selected organisms is: Streptomyces purpurascens
The enzyme appears in selected viruses and cellular organisms
Synonyms
aklavinone 12-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
aklavinone,NADPH:oxygen oxidoreductase (12-hydroxylating)
The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11-deoxy-beta-L-rhodomycinone + NADPH + H+ + O2
beta-rhodomycinone + NADP+ + H2O
show the reaction diagram
-
11-deoxy-L-rhodomycinone is a better substrate than aklavinone
-
-
?
aklavinone + NADH + H+ + O2
epsilon-rhodomycinone + NAD+ + H2O
show the reaction diagram
-
the enzyme participates in the biosynthesis of daunorubicin, doxorubicin and rhodomycins
-
-
?
aklavinone + NADPH + H+ + O2
epsilon-rhodomycinone + NADP+ + H2O
show the reaction diagram
additional information
?
-
-
no activity with decarbomethoxyaklavinone or 15-demethoxyaklavinone
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aklavinone + NADPH + H+ + O2
epsilon-rhodomycinone + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the enzyme contains a FAD-binding domain
FAD
-
the enzyme is a FAD monooxygenase
NADH
-
aklavinone-11-hydroxylase can use both NADH and NADPH as coenzyme but it is slowly inactivated in the presence of NADH
NADPH
-
aklavinone-11-hydroxylase can use both NADH and NADPH as coenzyme but it is slowly inactivated in the presence of NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
-
-
Phenylglyoxal
-
NADPH protects against inactivation of aklavinone-11-hydroxylase by phenylglyoxal
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
aklavinone
-
pH and temperature not specified in the publication
2
NADPH
-
pH and temperature not specified in the publication
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNRF_STREF
535
0
57437
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57436
-
x * 57436, calculated from sequence
60000
-
1 * 60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 57436, calculated from sequence
monomer
-
1 * 60000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of a ternary complex of this enzyme from Streptomyces purpurascens, RdmE, with FAD and the substrate aklavinone
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R373X
mutants at position Arg373 retain catalytic activity close to wild-type level
Y224F
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the gene in Streptomyces lividans
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niemi, J.; Wang, Y.; Airas, K.; Ylihonko, K.; Hakala, J.; Mäntsälä, P.
Characterization of aklavinone-11-hydroxylase from Streptomyces purpurascens
Biochim. Biophys. Acta
1430
57-64
1999
Streptomyces purpurascens
Manually annotated by BRENDA team
Wang, Y.; Niemi, J.; Mäntsälä, P.
Modification of aklavinone and aclacinomycins in vitro and in vivo by rhodomycin biosynthesis gene products
FEMS Microbiol. Lett.
208
117-122
2002
Streptomyces purpurascens
Manually annotated by BRENDA team
Niemi, J.; Mäntsälä, P.
Nucleotide sequences and expression of genes from Streptomyces purpurascens that cause the production of new anthracyclines in Streptomyces galilaeus
J. Bacteriol.
177
2942-2945
1995
Streptomyces purpurascens
Manually annotated by BRENDA team
Lindqvist, Y.; Koskiniemi, H.; Jansson, A.; Sandalova, T.; Schnell, R.; Liu, Z.; Mäntsälä, P.; Niemi, J.; Schneider, G.
Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis
J. Mol. Biol.
393
966-977
2009
Streptomyces purpurascens (Q54530)
Manually annotated by BRENDA team