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Information on EC 4.2.1.154 - tetracenomycin F2 cyclase
for references in articles please use BRENDA:EC4.2.1.154
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IUBMB Comments
The enzyme is involved in biosynthesis of the anthracycline antibiotic tetracenomycin C by the bacterium Streptomyces glaucescens.
The enzyme appears in viruses and cellular organisms
showSynonyms
tetracenomycin f2 cyclase, tcm f2 cyclase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Tcm F2 cyclase
tcmI
tcmI
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tetracenomycin F2 = tetracenomycin F1 + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
elloramycin biosynthesis, tetracenomycin C biosynthesis
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: -
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
Substrates: -
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: at pH 8.0 or higher, the enzyme catalyzes the cyclization of tetracenomycin F2 to tetracenomycin F1, while below pH 6.5, the enzyme catalyzes the cyclization of tetracenomycin F2 to 9-decarboxy-tetracenomycin F1
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: at pH 8.0 or higher, the enzyme catalyzes the cyclization of tetracenomycin F2 to tetracenomycin F1, while below pH 6.5, the enzyme catalyzes the cyclization of tetracenomycin F2 to 9-decarboxy-tetracenomycin F1
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: -
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
Substrates: -
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: at pH 8.0 or higher, the enzyme catalyzes the cyclization of tetracenomycin F2 to tetracenomycin F1, while below pH 6.5, the enzyme catalyzes the cyclization of tetracenomycin F2 to 9-decarboxy-tetracenomycin F1
Products: -
Products: -
?
tetracenomycin F2
tetracenomycin F1 + H2O
-
Substrates: at pH 8.0 or higher, the enzyme catalyzes the cyclization of tetracenomycin F2 to tetracenomycin F1, while below pH 6.5, the enzyme catalyzes the cyclization of tetracenomycin F2 to 9-decarboxy-tetracenomycin F1
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.155
tetracenomycin F2
wild type enzyme, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.191
tetracenomycin F2
mutant enzyme H51Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.203
tetracenomycin F2
mutant enzyme H26Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.732
tetracenomycin F2
mutant enzyme H26A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.816
tetracenomycin F2
mutant enzyme R40K, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.892
tetracenomycin F2
mutant enzyme H51A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
1.05
tetracenomycin F2
mutant enzymeD27N, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
1.2
tetracenomycin F2
mutant enzyme R40G, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0146
tetracenomycin F2
mutant enzyme R40G, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0192
tetracenomycin F2
mutant enzyme H26A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0198
tetracenomycin F2
mutant enzymeD27N, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0219
tetracenomycin F2
mutant enzyme H51A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.025
tetracenomycin F2
mutant enzyme R40K, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.131
tetracenomycin F2
mutant enzyme H26Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.136
tetracenomycin F2
mutant enzyme H51Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.142
tetracenomycin F2
wild type enzyme, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0121
tetracenomycin F2
mutant enzyme R40G, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0188
tetracenomycin F2
mutant enzymeD27N, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0245
tetracenomycin F2
mutant enzyme H51A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0262
tetracenomycin F2
mutant enzyme H26A, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.0306
tetracenomycin F2
mutant enzyme R40K, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.645
tetracenomycin F2
mutant enzyme H26Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.712
tetracenomycin F2
mutant enzyme H51Q, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
0.916
tetracenomycin F2
wild type enzyme, at 30Ā°C in 0.1 M Tris-HCl, pH 7.5
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A101RVT7_9ACTN
110
0
12480
TrEMBL
-
A0A385ZZJ8_9ACTN
223
0
25372
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
macroseeding method, using 1.4 M (NH4)2SO4, 50 mM HEPES, pH 7.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Mono Q column chromatography, phenyl-Superose gel filtration, Superose 6 gel filtration, and Sephacryl S-200 gel filtration
-
Q-Sepharose column chromatography, phenyl-Sepharose column chromatography, and MonoQ column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
brenda
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
brenda
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
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.154)
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Release 2023.1 (January 2023)
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