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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.1.154 - tetracenomycin F2 cyclase and Organism(s) Streptomyces glaucescens and UniProt Accession P39890

for references in articles please use BRENDA:EC4.2.1.154
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.154 tetracenomycin F2 cyclase
IUBMB Comments
The enzyme is involved in biosynthesis of the anthracycline antibiotic tetracenomycin C by the bacterium Streptomyces glaucescens.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces glaucescens
UNIPROT: P39890
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 glaucescens
The enzyme appears in selected viruses and cellular organisms
Synonyms
tetracenomycin f2 cyclase, tcm f2 cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tcm F2 cyclase
-
-
TcmI cyclase
-
-
SYSTEMATIC NAME
IUBMB Comments
tetracenomycin F2 hydro-lyase (tetracenomycin-F1-forming)
The enzyme is involved in biosynthesis of the anthracycline antibiotic tetracenomycin C by the bacterium Streptomyces glaucescens.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tetracenomycin F2
tetracenomycin F1 + H2O
show the reaction diagram
-
-
-
?
tetracenomycin F2
tetracenomycin F1 + H2O
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
tetracenomycin F2
tetracenomycin F1 + H2O
show the reaction diagram
-
-
-
?
tetracenomycin F2
tetracenomycin F1 + H2O
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.155 - 1.2
tetracenomycin F2
0.121
tetracenomycin F2
-
at pH 8.0 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0146 - 0.142
tetracenomycin F2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0121 - 0.916
tetracenomycin F2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000571
-
cell-free extract, at pH 8.0 and 30°C
0.309
-
after 541fold purification, at pH 8.0 and 30°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TCMI_STRGA
109
0
12861
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12500
-
3 * 12500, SDS-PAGE
12728
-
3 * 12728, calculated from amino acid sequence
37500
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
macroseeding method, using 1.4 M (NH4)2SO4, 50 mM HEPES, pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D27N
the mutant shows 14% activity compared to the wild type enzyme
H26A
the mutant shows 15% activity compared to the wild type enzyme
H26Q
the mutant shows 91% activity compared to the wild type enzyme
H51A
the mutant shows 16% activity compared to the wild type enzyme
H51Q
the mutant shows 96% activity compared to the wild type enzyme
R40G
the mutant shows 10% activity compared to the wild type enzyme
R40K
the mutant shows 16% activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography, phenyl-Sepharose column chromatography, and MonoQ column chromatography
ammonium sulfate precipitation, Mono Q column chromatography, phenyl-Superose gel filtration, Superose 6 gel filtration, and Sephacryl S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Summers, R.G.; Wendt-Pienkowski, E.; Motamedi, H.; Hutchinson, C.R.
The tcmVI region of the tetracenomycin C biosynthetic gene cluster of Streptomyces glaucescens encodes the tetracenomycin F1 monooxygenase, tetracenomycin F2 cyclase, and, most likely, a second cyclase
J. Bacteriol.
175
7571-7580
1993
Streptomyces glaucescens
Manually annotated by BRENDA team
Shen, B.; Hutchinson, C.R.
Tetracenomycin F2 cyclase: intramolecular aldol condensation in the biosynthesis of tetracenomycin C in Streptomyces glaucescens
Biochemistry
32
11149-11154
1993
Streptomyces glaucescens, Streptomyces glaucescens WMH1068
Manually annotated by BRENDA team
Thompson, T.B.; Katayama, K.; Watanabe, K.; Hutchinson, C.R.; Rayment, I.
Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase
J. Biol. Chem.
279
37956-37963
2004
Streptomyces glaucescens (P39890), Streptomyces glaucescens
Manually annotated by BRENDA team