Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.1.95 - aclacinomycin methylesterase and Organism(s) Streptomyces purpurascens and UniProt Accession Q54528

for references in articles please use BRENDA:EC3.1.1.95
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.95 aclacinomycin methylesterase
IUBMB Comments
The enzyme is involved in the modification of the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces purpurascens
UNIPROT: Q54528
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Streptomyces purpurascens
The enzyme appears in selected viruses and cellular organisms
Synonyms
aclacinomycin methylesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
aclacinomycin T acylhydrolase
The enzyme is involved in the modification of the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aclacinomycin T + H2O
15-demethylaclacinomycin T + methanol
show the reaction diagram
-
-
-
-
?
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
aclacinomycin T + H2O
15-demethylaclacinomycin T + methanol
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0155
aclacinomycin T
-
pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
169.4
-
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 45
-
30°C: 58% of maximal activity, 45°C: 87% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the modification of modify the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RDMC_STREF
298
0
31792
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
1 * 30000, SDS-PAGE
31729
-
1 * 31729, calculated from sequence
33000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion in hanging drops, crystal structures RdmC in complex with the product analogues 10-demethoxycarbonylaclacinomycin T and 10-decarboxymethylaclacinomycin A are determined to nominal resolutions of 1.45 and 1.95 A, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Streptomyces lividans TK24
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Niemi, J.; Airas, K.; Ylihonko, K.; Hakala, J.; Mntsl, P.
Modifications of aclacinomycin T by aclacinomycin methyl esterase (RdmC) and aclacinomycin-10-hydroxylase (RdmB) from Streptomyces purpurascens
Biochim. Biophys. Acta
1480
191-200
2000
Streptomyces purpurascens
Manually annotated by BRENDA team
Jansson, A.; Niemi, J.; Mntsl, P.; Schneider, G.
Crystal structure of aclacinomycin methylesterase with bound product analogues: implications for anthracycline recognition and mechanism
J. Biol. Chem.
278
39006-39013
2003
Streptomyces purpurascens (Q54528), Streptomyces purpurascens
Manually annotated by BRENDA team