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Literature summary for 1.1.1.35 extracted from

  • Filling, C.; Keller, B.; Hirschberg, D.; Marschall, H.U.; Joernvall, H.; Bennett, M.J.; Oppermann, U.
    Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency (2008), Biochem. Biophys. Res. Commun., 368, 6-11.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000058
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD II, at pH 8.0 Homo sapiens
0.000058
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD II, at pH 9.3 Homo sapiens
0.00009
-
NAD+ isozyme SCHAD II, at pH 7.0 Homo sapiens
0.0009
-
NADH isozyme SCHAD II, at pH 9.3 Homo sapiens
0.00119
-
NAD+ isozyme SCHAD I, at pH 7.0 Homo sapiens
0.00261
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD I, at pH 8.0 Homo sapiens
0.00529
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD I, at pH 8.5 Homo sapiens
0.0166
-
acetoacetyl-CoA isozyme SCHAD I, at pH 7.0 Homo sapiens
0.0222
-
acetoacetyl-CoA isozyme SCHAD I, at pH 8.0 Homo sapiens
0.0257
-
acetoacetyl-CoA isozyme SCHAD II, at pH 7.0 Homo sapiens
0.0315
-
acetoacetyl-CoA isozyme SCHAD II, at pH 8.0 Homo sapiens
0.0338
-
NADH isozyme SCHAD I, at pH 8.5 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-
muscle
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-hydroxybutyryl-CoA + NAD+
-
Homo sapiens acetoacetyl-CoA + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
L-3-hydroxybutyryl CoA dehydrogenase
-
Homo sapiens
SCHAD I isozyme Homo sapiens
SCHAD II isozyme Homo sapiens
short-chain hydroxyacyl CoA dehydrogenase
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21.3
-
acetoacetyl-CoA isozyme SCHAD II, at pH 8.0 Homo sapiens
23.8
-
acetoacetyl-CoA isozyme SCHAD II, at pH 7.0 Homo sapiens
176.7
-
NADH isozyme SCHAD I, at pH 8.5 Homo sapiens
375
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD I, at pH 8.5 Homo sapiens
510
-
NADH isozyme SCHAD II, at pH 9.3 Homo sapiens
533.3
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD I, at pH 8.0 Homo sapiens
643.3
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD II, at pH 8.0 Homo sapiens
681.7
-
acetoacetyl-CoA isozyme SCHAD I, at pH 8.0 Homo sapiens
705
-
NAD+ isozyme SCHAD II, at pH 7.0 Homo sapiens
1287
-
acetoacetyl-CoA isozyme SCHAD I, at pH 7.0 Homo sapiens
1420
-
(S)-3-hydroxybutyryl-CoA isozyme SCHAD II, at pH 9.3 Homo sapiens
1817
-
NAD+ isozyme SCHAD I, at pH 7.0 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
SCAD I and SCHAD II, pH optimum the reduction Homo sapiens
8.5
-
SCAD I, pH optimum for oxidation Homo sapiens
9.3
-
SCHAD II, pH optimum for oxidation Homo sapiens