Any feedback?
Information on EC 1.18.6.1 - nitrogenase and Organism(s) Clostridium pasteurianum and UniProt Accession P11347
for references in articles please use BRENDA:EC1.18.6.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.18.6.1 nitrogenaseIUBMB Comments
Requires Mg2+. The enzyme is a complex of two components (namely dinitrogen reductase and dinitrogenase). Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component. Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine. The reduction is initiated by formation of hydrogen in stoichiometric amounts . Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)]. The enzyme does not reduce CO (cf. EC 1.18.6.2, vanadium-dependent nitrogenase).
Specify your search results
Word Map
- 1.18.6.1
- nodule
- azotobacter
-
nitrogen-fixing
- vinelandii
-
diazotrophic
- acetylene
-
symbiotic
- klebsiella
- ammonia
- pneumoniae
- cyanobacterium
- rhizobium
- anabaena
- heterocysts
- nitrate
-
legume
-
n2-fixing
-
bacteroid
- hydrogenase
- epr
-
free-living
-
atmospheric
- nh3
- rubrum
- bradyrhizobium
- azospirillum
- rhodospirillum
- japonicum
- rhodobacter
- meliloti
-
rhizosphere
- nostoc
- capsulatus
- pasteurianum
- brasilense
-
microaerobic
- rhodopseudomonas
- leguminosarum
- leghemoglobin
- variabilis
- mgadp
-
carbide
-
dithionite-reduced
-
endor
-
biofertilizer
- flavodoxins
-
drag
-
symbioses
- bacteriochlorophyll
- synthesis
- agriculture
- energy production
-
anoxygenic
The taxonomic range for the selected organisms is: Clostridium pasteurianum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
4
+
8
+
+
16
+
16
=
4
+
+
2
+
16
+
16
Synonyms
nitrogenase, mofe protein, dinitrogenase, nifhdk, nifdk, mo-nitrogenase, mofe-protein, v-nitrogenase, nitrogenase mofe protein, n2ase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
4 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 4 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
ferredoxin:dinitrogen oxidoreductase (ATP-hydrolysing, molybdenum-dependent)
Requires Mg2+. The enzyme is a complex of two components (namely dinitrogen reductase and dinitrogenase). Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component. Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine. The reduction is initiated by formation of hydrogen in stoichiometric amounts [2]. Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia. In the absence of a suitable substrate, hydrogen is slowly formed. Ferredoxin may be replaced by flavodoxin [see EC 1.19.6.1 nitrogenase (flavodoxin)]. The enzyme does not reduce CO (cf. EC 1.18.6.2, vanadium-dependent nitrogenase).
CAS REGISTRY NUMBER
COMMENTARY
9013-04-1
-
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
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
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
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
structure models of Fe protein, MoFe protein, and MoFe-cofactor, and their metal centers, e.g. the [4Fe-4S] cluster based on crystallographic data, substrate binding and electron transfer
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mg2+
Molybdenum
Vanadium
-
characterization of the metal clusters in the nitrogenase vanadium-iron protein
additional information
Iron
contains iron and a Fe-Mo cofactor (the active site, a [7Fe:9S:Mo:C:R-homocitrate] cluster)
Mg2+
-
Mg2+ required for MgATP complex
Molybdenum
-
1-2 gatom per mol of MoFe protein , overview
Molybdenum
-
molybdenum metabolism, cofactor synthesis from nif genes , regulation and structure, overview
Molybdenum
-
MoFe-cofactor contains 2 clusters of composition [4Fe-3S] and [1Mo-3Fe-3S] that are brigded by 3 nonprotein ligands
Molybdenum
contains a Fe-Mo cofactor (the active site, a [7Fe:9S:Mo:C:R-homocitrate] cluster)
additional information
-
other metal ions, e.g. Cu2+, Mg2+, Zn2+, Ca2+, at levels of 1-2 atoms per mol detected in the MoFe protein, no evidence for specific requirement, except for Mg2+ in MgATP complex, of any of these metals
additional information
-
structure and organization of metal clusters
additional information
-
contains also an inactive MoFe protein species
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CO
-
noncompetitive inhibitor of N2, C2H2 and N3- reduction, no inhibition of H+ reduction
H2
-
competitive inhibitor of N2, no inhibition of N3-, C2H2, CN- or H+ reduction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
homocitrate
-
plays role in electron transfer at the [4Fe-4S] cluster to the MoFe-cofactor of the MoFe protein, can be substituted by erythro-fluorohomocitrate but not by threo-fluorohomocitrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview, different substrates
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
not established, whether the nitrogenase exists in vivo in a specific particle or whether the nitrogenase proteins are bound nonspecifically to the membranes of some cells
-
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
27500
51000
-
component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE
60000
additional information
27500
-
component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE
60000
-
component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
dimer
-
Fe protein is a dimer of 2 identical subunits, MW 27500-34600, various methods, overview
tetramer
-
component I Fe protein 2 * 27500 + component II MoFe protein 1 * 60000 + 1 * 51000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MoFe protein, crystallized in presence of approx. 5% w/v polyethylene glycol 6000 and 0.2-0.4 M MgCl2 under strictly anaerobic conditions, x-ray analysis
-
sitting drop vapor diffusion method, using 23% polyethylene glycol 3350, 0.2 M lithium citrate, and 5 mM sodium dithionite
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haaker, H.; Klugkist, J.
The bioenergetics of electron transport to nitrogenase
FEMS Microbiol. Rev.
46
57-71
1987
Azotobacter vinelandii, Anabaena cylindrica, Anabaena sp., Azospirillum sp., Azotobacter sp., Paenibacillus polymyxa, Chlorobium sp., Chromatium sp., Clostridium pasteurianum, Desulfovibrio sp., Frankia sp., Gloeothece sp., Klebsiella pneumoniae, Leptolyngbya boryana, Rhizobium leguminosarum, Rhizobium sp., Cereibacter sphaeroides, Rhodopseudomonas sp., Rhodospirillum rubrum, Rhizobium sp. ORS 571
-
Vignais, P.M.; Colbeau, A.; Willison, J.C.; Jouanneau, Y.
Hydrogenase, nitrogenase, and hydrogen metabolism in the photosynthetic bacteria
Adv. Microb. Physiol.
26
155-234
1985
Azotobacter vinelandii, Allochromatium vinosum, Clostridium pasteurianum, Klebsiella pneumoniae, Rhodobacter capsulatus, Rhodospirillum rubrum
Eady, R.R.
Isolation and characterization of various nitrogenases
Methods Enzymol.
69
753-778
1980
Azotobacter vinelandii, Allochromatium vinosum, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Klebsiella pneumoniae, Bradyrhizobium lupini, Rhodospirillum rubrum
-
Winter, H.C.; Burris, R.H.
Nitrogenase
Annu. Rev. Biochem.
45
409-426
1976
Azotobacter vinelandii, Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Klebsiella pneumoniae, Bradyrhizobium lupini, Rhodospirillum rubrum
Eady, R.R.; Postgate, J.R.
Nitrogenase
Nature
249
805-810
1974
Azotobacter vinelandii, Allochromatium vinosum, Anabaena cylindrica, Azotobacter chroococcum, Paenibacillus polymyxa, Bradyrhizobium japonicum, Clostridium pasteurianum, Corynebacterium flavescens, Desulfovibrio desulfuricans, Escherichia coli, Gloeocapsa sp., Klebsiella pneumoniae, Ornithopus sativus, Leptolyngbya boryana, Bradyrhizobium lupini, Rhizobium sp., Rhodospirillum rubrum, Escherichia coli C-M 74, Corynebacterium flavescens 301
Mortenson, L.E.; Thorneley, R.N.F.
Structure and function of nitrogenase
Annu. Rev. Biochem.
48
387-418
1979
Azotobacter vinelandii, Azotobacter chroococcum, Paenibacillus polymyxa, Clostridium pasteurianum, Klebsiella pneumoniae
Shah, V.K.; Ugalde, R.A.; Imperial, J.; Brill, W.J.
Molybdenum in nitrogenase
Annu. Rev. Biochem.
53
231-257
1984
Azotobacter vinelandii, Paenibacillus polymyxa, Clostridium pasteurianum, Klebsiella pneumoniae
Weininger, M.S.; Mortenson, L.E.
Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii
Proc. Natl. Acad. Sci. USA
79
379-380
1982
Azotobacter vinelandii, Clostridium pasteurianum
-
Mortenson, L.E.
Purification aof nitrogenase from Clostridium pasteurianum
Methods Enzymol.
24B
446-456
1972
Clostridium pasteurianum
Tso, M.Y.W.
Some properties of the nitrogenase proteins from Clostridium pasteurianum. Molecular weight, subunit structure, isoelectric point and EPR spectra
Arch. Microbiol.
99
71-80
1974
Clostridium pasteurianum
Zumft, W.G.; Mortenson, L.E.
The nitrogen-fixing complex of bacteria
Biochim. Biophys. Acta
416
1-52
1975
Azotobacter vinelandii, Chromatium sp., Clostridium pasteurianum, Klebsiella pneumoniae, Rhizobium sp.
Erickson, J.A.; Nyborg, A.C.; Johnson, J.L.; Truscott, S.M.; Gunn, A.; Nordmeyer, F.R.; Watt, G.D.
Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants That form the all-ferrous redox state of the Fe protein
Biochemistry
38
14279-14285
1999
Azotobacter vinelandii, Clostridium pasteurianum, Azotobacter vinelandii OP
Kim, J.; Rees, D.C.
Nitrogenase and biological nitrogen fixation
Biochemistry
33
389-397
1994
Azotobacter vinelandii, Azotobacter chroococcum, Clostridium pasteurianum
Morrison, C.N.; Hoy, J.A.; Zhang, L.; Einsle, O.; Rees, D.C.
Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites
Biochemistry
54
2052-2060
2015
Klebsiella pneumoniae (P00466 and P09772), Klebsiella pneumoniae, Clostridium pasteurianum (P00467 and P11347), Clostridium pasteurianum, Azotobacter vinelandii (P07328 and P07329), Azotobacter vinelandii
Morrison, C.N.; Spatzal, T.; Rees, D.C.
Reversible protonated resting state of the nitrogenase active site
J. Am. Chem. Soc.
139
10856-10862
2017
Azotobacter vinelandii, Clostridium pasteurianum
EXTERNAL LINKS (specific for EC-Number 1.18.6.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
