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Literature summary for 1.4.1.7 extracted from

  • Kretovich, W.L.; Stepanovich, K.M.
    The enzyme catalyzing hydroxypyruvate reductive amination (1966), Izv. Akad. Nauk SSSR Ser. Biol., 2, 295-301.
No PubMed abstract available

General Stability

General Stability Organism
very labile enzyme, loses its activity when exposed to dialysis or weak heating Petroselinum crispum

Inhibitors

Inhibitors Comment Organism Structure
p-chloromercurybenzoate completely inhibited at 0.005 mM Petroselinum crispum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0005
-
Hydroxypyruvate
-
Petroselinum crispum
0.015
-
NH3
-
Petroselinum crispum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine + H2O + NAD+ Petroselinum crispum
-
3-hydroxypyruvate + NH3 + NADH
-
?

Organism

Organism UniProt Comment Textmining
Petroselinum crispum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
isolated from an albumin fraction, purified on Sephadex G-76, subsequently on DEAE-cellulose Petroselinum crispum

Source Tissue

Source Tissue Comment Organism Textmining
leaf green leaves Petroselinum crispum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + H2O + NAD+
-
Petroselinum crispum 3-hydroxypyruvate + NH3 + NADH
-
?
additional information no substrates in presence of NADH: alpha-ketoglutarate, oxaloacetate, glyoxylate, or pyruvate Petroselinum crispum ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
in phosphate buffer Petroselinum crispum

Cofactor

Cofactor Comment Organism Structure
NADH specific for NADH, does not react with NADPH, strictly specific for hydroxypyruvate in presence of NADH Petroselinum crispum