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show all sequences of 1.1.1.275

Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors

Haft, D.H.; Pierce, P.G.; Mayclin, S.J.; Sullivan, A.; Gardberg, A.S.; Abendroth, J.; Begley, D.W.; Phan, I.Q.; Staker, B.L.; Myler, P.J.; Marathias, V.M.; Lorimer, D.D.; Edwards, T.E.; Sci. Rep. 7, 41074 (2017)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover; to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium subsp. paratuberculosis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium avium
A0A0H2ZTN5
-
-
Mycobacterium avium
A0A0H2ZU39
-
-
Mycobacterium avium
A0A0H2ZV91
-
-
Mycobacterium avium
A0A0H2ZWY3
-
-
Mycobacterium avium
A0A0H2ZYS9
-
-
Mycobacterium avium 104
A0A0H2ZTN5
-
-
Mycobacterium avium 104
A0A0H2ZU39
-
-
Mycobacterium avium 104
A0A0H2ZV91
-
-
Mycobacterium avium 104
A0A0H2ZWY3
-
-
Mycobacterium avium 104
A0A0H2ZYS9
-
-
Mycobacterium avium subsp. paratuberculosis
Q73SC8
-
-
Mycobacterium avium subsp. paratuberculosis ATCC BAA-968
Q73SC8
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium
to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium subsp. paratuberculosis
to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium
to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium
to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover
Mycobacterium avium
Other publictions for EC 1.1.1.275
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741432
Haft
Mycofactocin-associated mycoba ...
Mycobacterium avium 104, Mycobacterium avium, Mycobacterium avium subsp. paratuberculosis, Mycobacterium avium subsp. paratuberculosis ATCC BAA-968
Sci. Rep.
7
41074
2017
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2
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12
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6
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639355
Duetz
Biotransformation of D-limonen ...
Rhodococcus opacus, Rhodococcus opacus PWD4 / DSM 44313
Appl. Environ. Microbiol.
67
2829-2832
2001
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1
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2
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2
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639021
Bouwmeester
Biosynthesis of the monoterpen ...
Carum carvi
Plant Physiol.
117
901-912
1998
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1
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1
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7
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7
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