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Enzyme Nomenclature
Information on EC 1.14.19.70 - mycocyclosin synthase
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EC Tree
1.14.19.70 mycocyclosin synthaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalysing an oxidative reaction that does not incorporate oxygen into the product.
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Word Map
- 1.14.19.70
- tuberculosis
- heme
- azole
-
antimycobacterial
- clotrimazole
- triazole
-
antituberculosis
-
fragment-based
- econazole
- fluconazole
- medicine
- isoniazid
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
2
+
=
+
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
+
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
2
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP121
EC 1.14.21.9
-
-
formerly
-
rv2276
CYP121
-
-
-
-
CYP121
-
rv2276
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
cyclo(L-tyrosyl-L-tyrosyl),reduced ferredoxin:oxygen oxidoreductase (diarylbridge-forming)
A cytochrome P-450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalysing an oxidative reaction that does not incorporate oxygen into the product.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
cyclo-(L-tyrosyl-DOPA) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
transformation of cyclo-(L-tyrosyl-DOPA) by CYP121 is very slow, 91% of the compound remains after 1 h of incubation with CYP121
-
-
?
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
98% of the compound remains after 1 h incubation with CYP121
-
-
?
(3S,6S)-3,6-bis(4-hydroxybenzyl)piperazin-2-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
98% of the compound remains after 1 h incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
the rate of transformation of cyclo(L-tyrosyl-L-phenylalanyl) is very slow, with about 98% of compound remaining after 1 h of incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-phenylalanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
the rate of transformation of cyclo(L-tyrosyl-L-phenylalanyl) is very slow, with about 98% of compound remaining after 1 h of incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
about 50% of the initial compound remains after a 1 h incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-tryptophanyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
?
about 50% of the initial compound remains after a 1 h incubation with CYP121
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
100% transformation
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
100% transformation
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
classical and quantum based computer simulation methods are used to study in detail the reaction mechanism. Substrate binding promotes formation of the initial oxy complex. Compound I is responsible for first Tyr radical formation, and that the second Tyr radical is formed subsequently, through a proton-coupled electron transfer reaction, promoted by the presence of key residue Arg386. The final C-C coupling reaction possibly occurs in bulk solution, thus yielding the product in one oxygen reduction cycle
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
study of substrate binding kinetics
-
-
?
additional information
?
-
no activity with cyclo(L-tyrosyl-L-alanyl)
-
-
?
additional information
?
-
-
no activity with cyclo(L-tyrosyl-L-alanyl)
-
-
?
additional information
?
-
no activity with cyclo(L-tyrosyl-L-alanyl)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2
mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome P450
CYP121 is a highly specific cytochrome P450
-
cytochrome P450
a cytochrome P450 enzyme. Structural, spectroscopic, and kinetic experiments are applied to investigate the equilibria among various heme states as a function of pH and temperature
-
cytochrome P450
a plausible free radicalbased mechanisms for the CC bond coupling reaction is proposed
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibited by cyclo(L-Tyr-L-Leu) and cyclo(L-Tyr-L-Met)
-
additional information
-
not inhibited by cyclo(L-Tyr-L-Leu) and cyclo(L-Tyr-L-Met)
-
additional information
the cyclo-dipeptide substrates of the essential Mycobacterium tuberculosis enzyme CYP121 are deconstructed into their component fragments and screened against the enzyme
-
additional information
biophysical screening procedure employing a focused library of privileged scaffolds, which ultimately lead to the discovery of novel CYP121 inhibitors
-
additional information
-
biophysical screening procedure employing a focused library of privileged scaffolds, which ultimately lead to the discovery of novel CYP121 inhibitors
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The Mycobacterium tuberculosis cytochromes P450: physiology, biochemistry & molecular intervention.
Tuberculosis
Application of Fragment Screening and Merging to the Discovery of Inhibitors of the Mycobacterium tuberculosis Cytochrome?P450 CYP121.
Tuberculosis
Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450.
Tuberculosis
Azole antifungals are potent inhibitors of cytochrome P450 mono-oxygenases and bacterial growth in mycobacteria and streptomycetes.
Tuberculosis
Characterization of active site structure in CYP121. A cytochrome P450 essential for viability of Mycobacterium tuberculosis H37Rv.
Tuberculosis
Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway.
Tuberculosis
Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode.
Tuberculosis
Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis.
Tuberculosis
CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen.
Tuberculosis
Expression, purification and spectroscopic characterization of the cytochrome P450 CYP121 from Mycobacterium tuberculosis.
Tuberculosis
Fragment-Based Approaches to the Development of Mycobacterium tuberculosis CYP121 Inhibitors.
Tuberculosis
Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis.
Tuberculosis
Molecular docking of azole drugs and their analogs on CYP121 of Mycobacterium tuberculosis.
Tuberculosis
Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs.
Tuberculosis
Nanoelectrospray ionization mass spectrometric study of Mycobacterium tuberculosis CYP121-ligand interactions.
Tuberculosis
New Application of 1,2,4-Triazole Derivatives as Antitubercular Agents. Structure, In Vitro Screening and Docking Studies.
Tuberculosis
Overcoming the Limitations of Fragment Merging: Rescuing a Strained Merged Fragment Series Targeting Mycobacterium tuberculosis CYP121.
Tuberculosis
Potential drug targets in the Mycobacterium tuberculosis cytochrome P450 system.
Tuberculosis
Probing Ligand Exchange in the P450 Enzyme CYP121 from Mycobacterium tuberculosis: Dynamic Equilibrium of the Distal Heme Ligand as a Function of pH and Temperature.
Tuberculosis
QM/MM study of the C-C coupling reaction mechanism of CYP121, an essential Cytochrome p450 of Mycobacterium tuberculosis.
Tuberculosis
Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1. Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium.
Tuberculosis
Spirooxindoles as novel 3D-fragment scaffolds: Synthesis and screening against CYP121 from M. tuberculosis.
Tuberculosis
Structure-Activity Relationship and Mode-Of-Action Studies Highlight 1-(4-Biphenylylmethyl)-1H-imidazole-Derived Small Molecules as Potent CYP121 Inhibitors.
Tuberculosis
Structure-Activity Relationships of cyclo(l-Tyrosyl-l-tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct.
Tuberculosis
Structure-based discovery of novel inhibitors of Mycobacterium tuberculosis CYP121 from Indonesian natural products.
Tuberculosis
Substrate and reaction specificity of Mycobacterium tuberculosis cytochrome P450 CYP121: insights from biochemical studies and crystal structures.
Tuberculosis
Substrate-Assisted Hydroxylation and O-Demethylation in the Peroxidase-like Cytochrome P450 Enzyme CYP121.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen
physiological function
physiological function
the enzyme is essential for bacterial viability
physiological function
-
the enzyme is essential for bacterial viability
-
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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). CP121_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
396
0
43256
Swiss-Prot
-
CP121_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
396
0
43256
Swiss-Prot
-
A0A2K8PFG9_STRLA
416
1
45523
TrEMBL
-
CP121_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
396
0
43256
Swiss-Prot
-
CP121_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
396
0
43256
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44962
2 * 44962, calculated from amino acid sequence, CYP121 is a predominantly dimeric protein, with a minor monomeric form present
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homohexamer
homodimer
2 * 44962, calculated from amino acid sequence, CYP121 is a predominantly dimeric protein, with a minor monomeric form present
homodimer
-
2 * 44962, calculated from amino acid sequence, CYP121 is a predominantly dimeric protein, with a minor monomeric form present
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fluconazole-bound CYP121, sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3350 and 0.2 M NaSCN
in complex with cyclo(L-tyrosyl-L-tyrosyl), sitting drop vapor diffusion method
ligand-bound enzyme, sitting drop vapor diffusion method, using in 100 mM Na-MES bufferat pH 5.0-5.5 and 1.6-2.2 M (NH4)2SO4, at 6°C
native enzyme or in complex with iodopyrazole, PtCN, K2PtCl4, or Hg(NO3)2, vapor diffusion method, using 30% (w/v) polyethylene glycol 8000, 0.2 M ammonium sulfate, pH 6.5
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and hydroxyapatite column chromatography
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and hydroxyapatite resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli HMS174 (DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
medicine
CYP121 is a potential target for the treatment of Mycobacterium tuberculosis infections
medicine
the CYP121 gene is essential for survival of Mycobacterium tuberculosis in vitro and the enzyme is believed to be the molecular target responsible for the anti-tubercular efficacy of azole antifungal compounds pharmacology
medicine
-
CYP121 is a potential target for the treatment of Mycobacterium tuberculosis infections
-
pharmacology
CYP121 is a potential target for the treatment of Mycobacterium tuberculosis infections
pharmacology
-
CYP121 is a potential target for the treatment of Mycobacterium tuberculosis infections
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duffell, K.M.; Hudson, S.A.; McLean, K.J.; Munro, A.W.; Abell, C.; Matak-Vinkovic, D.
Nanoelectrospray ionization mass spectrometric study of Mycobacterium tuberculosis CYP121-ligand interactions
Anal. Chem.
85
5707-5714
2013
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Hudson, S.; McLean, K.; Surade, S.; Yang, Y.; Leys, D.; Ciulli, A.; Munro, A.; Abell, C.
Application of fragment screening and merging to the discovery of inhibitors of the Mycobacterium tuberculosis cytochrome P450 CYP121
Angew. Chem. Int. Ed. Engl.
51
9311-9316
2012
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
McLean, K.J.; Dunford, A.J.; Sabri, M.; Neeli, R.; Girvan, H.M.; Balding, P.R.; Leys, D.; Seward, H.E.; Marshall, K.R.; Munro, A.W.
CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen
Biochem. Soc. Trans.
34
1178-1182
2006
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Sundaramurthi, J.C.; Kumar, S.; Silambuchelvi, K.; Hanna, L.E.
Molecular docking of azole drugs and their analogs on CYP121 of Mycobacterium tuberculosis
Bioinformation
7
130-133
2011
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Leys, D.; Mowat, C.G.; McLean, K.J.; Richmond, A.; Chapman, S.K.; Walkinshaw, M.D.; Munro, A.W.
Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450
J. Biol. Chem.
278
5141-5147
2003
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Seward, H.E.; Roujeinikova, A.; McLean, K.J.; Munro, A.W.; Leys, D.
Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode
J. Biol. Chem.
281
39437-39443
2006
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Fonvielle, M.; Le Du, M.H.; Lequin, O.; Lecoq, A.; Jacquet, M.; Thai, R.; Dubois, S.; Grach, G.; Gondry, M.; Belin, P.
Substrate and reaction specificity of Mycobacterium tuberculosis cytochrome P450 CYP121: insights from biochemical studies and crystal structures
J. Biol. Chem.
288
17347-17359
2013
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
McLean, K.J.; Cheesman, M.R.; Rivers, S.L.; Richmond, A.; Leys, D.; Chapman, S.K.; Reid, G.A.; Price, N.C.; Kelly, S.M.; Clarkson, J.; Smith, W.E.; Munro, A.W.
Expression, purification and spectroscopic characterization of the cytochrome P450 CYP121 from Mycobacterium tuberculosis
J. Inorg. Biochem.
91
527-541
2002
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Belin, P.; Le Du, M.H.; Fielding, A.; Lequin, O.; Jacquet, M.; Charbonnier, J.B.; Lecoq, A.; Thai, R.; Courcon, M.; Masson, C.; Dugave, C.; Genet, R.; Pernodet, J.L.; Gondry, M.
Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis
Proc. Natl. Acad. Sci. USA
106
7426-7431
2009
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Kavanagh, M.E.; Gray, J.L.; Gilbert, S.H.; Coyne, A.G.; McLean, K.J.; Davis, H.J.; Munro, A.W.; Abell, C.
Substrate fragmentation for the design of M. tuberculosis CYP121 inhibitors
ChemMedChem
11
1924-1935
2016
Mycobacterium tuberculosis (P9WPP7)
brenda
Brengel, C.; Thomann, A.; Schifrin, A.; Allegretta, G.; Kamal, A.A.M.; Haupenthal, J.; Schnorr, I.; Cho, S.H.; Franzblau, S.G.; Empting, M.; Eberhard, J.; Hartmann, R.W.
Biophysical screening of a focused library for the discovery of CYP121 inhibitors as novel antimycobacterials
ChemMedChem
12
1616-1626
2017
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP7)
brenda
Fielding, A.J.; Dornevil, K.; Ma, L.; Davis, I.; Liu, A.
Probing ligand exchange in the P450 enzyme CYP121 from Mycobacterium tuberculosis Dynamic equilibrium of the distal heme ligand as a function of pH and temperature
J. Am. Chem. Soc.
139
17484-17499
2017
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis
brenda
Dornevil, K.; Davis, I.; Fielding, A.J.; Terrell, J.R.; Ma, L.; Liu, A.
Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway
J. Biol. Chem.
292
13645-13657
2017
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis
brenda
Dumas, V.; Defelipe, L.; Petruk, A.; Turjanski, A.; Marti, M.
QM/MM study of the C-C coupling reaction mechanism of CYP121, an essential cytochrome p450 of Mycobacterium tuberculosis
Proteins
82
1004-1021
2014
Mycobacterium tuberculosis (P9WPP7), Mycobacterium tuberculosis
brenda
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