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Literature summary for 1.12.98.4 extracted from

  • Childers, S.E.; Noll, K.M.
    Characterization and regulation of sulfur reductase activity in Thermotoga neapolitana (1994), Appl. Environ. Microbiol., 60, 2622-2626.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.12.98.4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
 Polysulfide PDH Thermotoga neapolitana

Organism

Organism UniProt Comment Textmining
Thermotoga neapolitana
-
-
-

Oxidation Stability

Oxidation Stability Organism
PDH activity is oxygen labile in crude extracts Thermotoga neapolitana

Reaction

Reaction Comment Organism Reaction ID
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1 two enzymes: hydrogenase with sulfur reductase activity and an NADPH-utilizing polysulfide dehydrogenase are detected Thermotoga neapolitana
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 spec. act. for the PDH are 12 to 48fold higher than for sulfhydrogenase Thermotoga neapolitana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
disulfide + electron donor cystine and cystamine, minimal activities, PDH Thermotoga neapolitana H2S
-
 ?
polysulfide + electron donor highest activity, NADH and NADPH as electron donors for PDH, hydrogen alone can reduce polysulfide via sulfhydrogenase, but the amount of this activity is minimal compared with that of PDH Thermotoga neapolitana H2S + oxidized electron donor
-
 ?
sulfur + electron donor electron donor: NADH or NAPDH Thermotoga neapolitana H2S + oxidized electron donor
-
 ?

Synonyms

Synonyms Comment Organism
polysulfide dehydrogenase PDH Thermotoga neapolitana
sulfhydrogenase homology of hydrogenase and sulfur reductase Thermotoga neapolitana