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Literature summary for 1.1.1.185 extracted from

  • Burgos, J.; Sarmiento, R.M.
    L-Glycol dehydrogenase from hen muscle (1982), Methods Enzymol., 89, 523-526.
    View publication on PubMed

General Stability

General Stability Organism
easily inactivated in high molarity buffers Gallus gallus
very stable in both water and low molarity buffers of pH 7 at 0-4┬░C Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
acetone pI 7.2 form Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
hen
-

Purification (Commentary)

Purification (Comment) Organism
3 enzyme forms: pI 7.2, pI 6.2 and pI 4.8 Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+ glyoxal reduction by enzyme form pI 7.2 follows ordered bi-bi mechanism in which the coenzyme is the first substrate to bind to the enzyme Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
0.4
-
-
Gallus gallus

Storage Stability

Storage Stability Organism
-18┬░C, enzyme at any stage of purification Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
R1-CO-CHOH-R2 + NAD(P)H
-
Gallus gallus R1-CHOH-CHOH-R2 + NAD(P)+
-
r

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6.6
-
Gallus gallus

pH Stability

pH Stability pH Stability Maximum Comment Organism
7
-
very stable in both water and low molarity buffers of pH 7 at 0-4┬░C Gallus gallus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Gallus gallus
NADH
-
Gallus gallus
NADPH
-
Gallus gallus