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Literature summary for 1.18.6.1 extracted from

  • Soboh, B.; Boyd, E.S.; Zhao, D.; Peters, J.W.; Rubio, L.M.
    Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB-co at its active site (2010), FEBS Lett., 584, 1487-1492.
    View publication on PubMed
Search for more literature for 1.18.6.1

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis, overview Klebsiella pneumoniae

Protein Variants

Protein Variants Comment Organism
additional information generation of a chimeric enzyme NifDK/NifB-co in which the active site iron-molybdenum cofactor is replaced by NifB-co. NifB is a S-adenosyl-L-methionine radical enzyme that functions in the synthesis of NifB-co, an early precursor to FeMo-cofactor. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3 Klebsiella pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe in the active site iron-molybdenum cofactor, and as 4Fe-4S cluster in the Fe protein Klebsiella pneumoniae
Mo in the active site iron-molybdenum cofactor Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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-
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Klebsiella pneumoniae UN1217
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-
-

Purification (Commentary)

Purification (Comment) Organism
native NifDK by gel filtration and affinity chromatography on a NifB resin, elution as NifDK/NifB-co complex Klebsiella pneumoniae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 comparison of ATP consumption coupled to H2 production by recombinant NifDK/NifB-co and by NifDK, overview Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3 Klebsiella pneumoniae ?
-
 ?
additional information substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3 Klebsiella pneumoniae UN1217 ?
-
 ?

Synonyms

Synonyms Comment Organism
molybdenum nitrogenase
-
 Klebsiella pneumoniae
NifDK
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 Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Klebsiella pneumoniae
iron-molybdenum cofactor located at the active site in the MoFe protein Klebsiella pneumoniae

General Information

General Information Comment Organism
evolution substrate specificity and evolutionary implications of a recombinant chimeric NifDK enzyme carrying NifB-co at its active site, NifDK/NifB-co, overview Klebsiella pneumoniae
physiological function the conversion of N2 into NH3 is catalyzed by the nitrogenase enzyme, which is composed of two metalloproteins: NifDK, also termed dinitrogenase or MoFe protein, and NifH, also termed dinitrogenase reductase or Fe protein Klebsiella pneumoniae