BRENDA - Enzyme Database show
show all sequences of 1.18.6.2

Structural genes for the vanadium nitrogenase from Azotobacter chroococcum

Robson, R.; Woodley, P.; Pau, R.; Eady, R.; EMBO J. 8, 1217-1224 (1989)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter chroococcum
P15332 and P15334 and P15333
P15332 i.e. subunit VnfD, P15334 i.e. subunit VnfK, P15333 i.e. subunit VnfG
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Azotobacter chroococcum MCD1
P15332 and P15334 and P15333
P15332 i.e. subunit VnfD, P15334 i.e. subunit VnfK, P15333 i.e. subunit VnfG
-
Subunits
Subunits
Commentary
Organism
?
x * 53793, subunit VnfD, x * 52724, subunit VnfK, x * 13274, subunit vnfG, calculated
Azotobacter chroococcum
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 53793, subunit VnfD, x * 52724, subunit VnfK, x * 13274, subunit vnfG, calculated
Azotobacter chroococcum
Expression
Organism
Commentary
Expression
Azotobacter chroococcum
genes for the three subunits vnJD (alpha), vnfG (delta) and vnfK (beta) are contiguous and form an operon whose transcription is repressed in response to ammonia
additional information
General Information
General Information
Commentary
Organism
physiological function
a deletion in the VnfD, VnfG and VnfK gene cluster prevents V-dependent nitrogen fixation. A strain defective in both V-nitrogenase and Mo-nitrogenase (EC 1.18.6.1) structural genes shows no residual nitrogen fixing capacity
Azotobacter chroococcum
General Information (protein specific)
General Information
Commentary
Organism
physiological function
a deletion in the VnfD, VnfG and VnfK gene cluster prevents V-dependent nitrogen fixation. A strain defective in both V-nitrogenase and Mo-nitrogenase (EC 1.18.6.1) structural genes shows no residual nitrogen fixing capacity
Azotobacter chroococcum
Expression (protein specific)
Organism
Commentary
Expression
Azotobacter chroococcum
genes for the three subunits vnJD (alpha), vnfG (delta) and vnfK (beta) are contiguous and form an operon whose transcription is repressed in response to ammonia
additional information
Other publictions for EC 1.18.6.2
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)
745388
Sippel
Production and isolation of v ...
Azotobacter vinelandii
J. Biol. Inorg. Chem.
22
161-168
2017
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745846
Sippel
The structure of vanadium nit ...
Azotobacter vinelandii
Nat. Chem. Biol.
13
956-960
2017
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744020
Lee
Tracing the hydrogen source o ...
Azotobacter vinelandii
Angew. Chem. Int. Ed. Engl.
50
5545-5547
2011
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746492
Lee
Vanadium nitrogenase reduces ...
Azotobacter vinelandii
Science
329
642
2010
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744180
Boison
The rice field cyanobacteria ...
Anabaena azotica, Anabaena azotica FACHB-118
Arch. Microbiol.
186
367-376
2006
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745204
Ruettimann-Johnson
VnfY is required for full act ...
Azotobacter vinelandii, Azotobacter vinelandii DJ
J. Bacteriol.
185
2383-2386
2003
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745197
Lyons
Characterization of nifB, nif ...
Trichormus variabilis
J. Bacteriol.
177
1570-1575
1995
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744261
Dilworth
The molybdenum and vanadium n ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
Biochem. J.
289
395-400
1993
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744007
Dilworth
Correction for creatine inter ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
Anal. Biochem.
207
6-10
1992
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744260
Thorneley
Vanadium nitrogenase of Azoto ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
Biochem. J.
257
789-794
1989
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744787
Robson
Structural genes for the vana ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
EMBO J.
8
1217-1224
1989
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744258
Eady
The vanadium nitrogenase of A ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
Biochem. J.
256
189-196
1988
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744259
Miller
Molybdenum and vanadium nitro ...
Azotobacter chroococcum
Biochem. J.
256
429-432
1988
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744257
Eady
The vanadium nitrogenase of A ...
Azotobacter chroococcum, Azotobacter chroococcum MCD1
Biochem. J.
244
197-207
1987
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