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Information on EC 1.14.19.8 - pentalenolactone synthase
for references in articles please use BRENDA:EC1.14.19.8
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
1.14.19.8 pentalenolactone synthase
IUBMB Comments
A heme-thiolate protein (P-450). Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
+
2
+
2
=
+
2
+
2
Synonyms
cyp161c2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.3.7.10
-
-
formerly
-
penM
pntM
penM
-
-
-
-
pntM
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+ = pentalenolactone + 2 oxidized ferredoxin + 2 H2O
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+ = pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
-
-
-
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+ = pentalenolactone + 2 oxidized ferredoxin + 2 H2O
molecular reaction mechanism, overview
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PATHWAY SOURCE
PATHWAYS
MetaCyc
pentalenolactone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
pentalenolactone-F:oxidized-ferredoxin oxidoreductase (pentalenolactone forming)
A heme-thiolate protein (P-450). Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
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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
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
Substrates: -
Products: -
Products: -
ir
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
Substrates: apparent ability of PntM to catalyze an exclusive carbocation-based oxidative rearrangement
Products: -
Products: -
?
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
Substrates: -
Products: -
Products: -
ir
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
Substrates: -
Products: -
Products: -
ir
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
Substrates: -
Products: -
Products: -
ir
pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+
pentalenolactone + 2 oxidized ferredoxin + 2 H2O
-
Substrates: -
Products: -
Products: -
ir
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with substrate analogue 6,7-dihydropentalenolactone, because the C1 carbocation is not anchimerically stabilized by the 6,7-double bond of pentalenolactone F. Enzyme-ligand interaction via three residues, F232, M77, and M81 that are unique to PntM and its orthologues and absent from essentially all other P450s
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with substrate analogue 6,7-dihydropentalenolactone, because the C1 carbocation is not anchimerically stabilized by the 6,7-double bond of pentalenolactone F. Enzyme-ligand interaction via three residues, F232, M77, and M81 that are unique to PntM and its orthologues and absent from essentially all other P450s
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
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
pentalenolactone F + O2 + NADPH + H+
pentalenolactone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
pentalenolactone F
recombinant wild-type enzyme, pH 8.0, 30°C
0.28
pentalenolactone F
recombinant mutant M81C-2-mercaptoethanol conjugate, pH 8.0, 30°C
0.34
pentalenolactone F
-
at 30°C, pH not specified in the publication
additional information
additional information
steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00142
pentalenolactone F
recombinant mutant M81C-2-mercaptoethanol conjugate, pH 8.0, 30°C
0.03
pentalenolactone F
recombinant wild-type enzyme, pH 8.0, 30°C
10.5
pentalenolactone F
-
at 30°C, pH not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0051
pentalenolactone F
recombinant mutant M81C-2-mercaptoethanol conjugate, pH 8.0, 30°C
0.83
pentalenolactone F
recombinant wild-type enzyme, pH 8.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme catalyzes the oxidative rearrangement in the final step of the sesquiterpenoid antibiotic pentalenolactone biosynthesis
additional information
additional information
structure analysis of free enzyme and ligand bound enzyme, detailed overview. The topology of PntM undergoes minimal changes upon binding of ligands
additional information
-
structure analysis of free enzyme and ligand bound enzyme, detailed overview. The topology of PntM undergoes minimal changes upon binding of ligands
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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). A0A852V0D4_9ACTN
385
0
42369
TrEMBL
-
A0A4P7CA93_9PSEU
392
0
43085
TrEMBL
-
A0A852TW66_9ACTN
390
0
42415
TrEMBL
-
A0A1L7FCZ9_9PSEU
395
0
42976
TrEMBL
-
A0A1D8C164_9PSEU
391
1
43280
TrEMBL
-
A0A2N9BJN2_STRCX
403
0
44540
TrEMBL
-
A0A1D8C184_9PSEU
399
0
43843
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
structure analysis of free enzyme and ligand bound enzyme, detailed overview
additional information
-
structure analysis of free enzyme and ligand bound enzyme, detailed overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified wild-type enzyme enzyme PntM substrate-free, and PntM with bound substrate pentalenolactone F, product pentalenolactone, and substrate analogue 6,7-dihydropentalenolactone, and recombinant PntM F232L, M77S, M81A, M81C, and M81C-BME mutants with bound pentalenolactone F, sitting drop vapor diffusion method, mixing of 0.001 ml of 16.8 mg/mL protein in 10 mM Tris-HCl, 15 mM NaCl, and 10% glycerol, with 0.001 ml of reservoir solution containing 1.2 M sodium citrate, 10% glycerol, and 100 mM bicine, pH 9.0, 15°C, followed by cross-microseeding technique, X-ray diffraction structure determination and analysis at 1.54 A and 2.06-2.12 A resolution, respectively, molecular replacement using the crystal structure of polyene macrolide epoxidase PimD, PDB ID 2X9P, as search model
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F232A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F232G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F232H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F232L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F232Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
M77S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
M81A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
M81C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA resin column chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography, tag cleavage by thrombin, another step of nickel affinity chromatography, and gel filtration of the eluate, followed by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene CYP161C2 or pntM, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription is activated by the PenR protein
transcription is activated by the PntR protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tetzlaff, C.N.; You, Z.; Cane, D.E.; Takamatsu, S.; Omura, S.; Ikeda, H.
A gene cluster for biosynthesis of the sesquiterpenoid antibiotic pentalenolactone in Streptomyces avermitilis
Biochemistry
45
6179-6186
2006
Streptomyces avermitilis
brenda
Zhu, D.; Seo, M.J.; Ikeda, H.; Cane, D.E.
Genome mining in Streptomyces. Discovery of an unprecedented P450-catalyzed oxidative rearrangement that is the final step in the biosynthesis of pentalenolactone
J. Am. Chem. Soc.
133
2128-2131
2011
Streptomyces arenae, Streptomyces arenae TUE469, Streptomyces exfoliatus, Streptomyces exfoliatus UC5319
brenda
Zhu, D.; Wang, Y.; Zhang, M.; Ikeda, H.; Deng, Z.; Cane, D.E.
Product-mediated regulation of pentalenolactone biosynthesis in Streptomyces species by the MarR/SlyA family activators PenR and PntR
J. Bacteriol.
195
1255-1266
2013
Streptomyces arenae, Streptomyces arenae TUE469, Streptomyces exfoliatus, Streptomyces exfoliatus UC5319
brenda
Duan, L.; Jogl, G.; Cane, D.
The cytochrome P450-catalyzed oxidative rearrangement in the final step of pentalenolactone biosynthesis substrate structure determines mechanism
J. Am. Chem. Soc.
138
12678-12689
2016
Streptomyces arenae (E3VWI3), Streptomyces arenae
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.19.8)
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Release 2023.1 (January 2023)
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