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Literature summary for 1.1.1.79 extracted from

  • Duan, X.; Hu, S.; Zhou, P.; Zhou, Y.; Liu, Y.; Jiang, Z.
    Characterization and crystal structure of a first fungal glyoxylate reductase from Paecilomyes thermophila (2014), Enzyme Microb. Technol., 60, 72-79.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene PtGR, DNa and mino acid seuence determination and analysis, sequence comparisons, recombinant expresssion of His-tagged enzyme in Escherichia coli strain BL21 Paecilomyces sp. 'thermophila'

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution Paecilomyces sp. 'thermophila'

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1
-
glyoxylate pH 7.5, 50°C, recombinant enzyme, with NADPH Paecilomyces sp. 'thermophila'

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
-
Paecilomyces sp. 'thermophila'
78000
-
recombinant enzyme, gel filtration Paecilomyces sp. 'thermophila'

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycolate + NADP+ Paecilomyces sp. 'thermophila'
-
glyoxylate + NADPH + H+
-
?
glycolate + NADP+ Paecilomyces sp. 'thermophila' J18
-
glyoxylate + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Paecilomyces sp. 'thermophila' A0A0H3U0Y7
-
-
Paecilomyces sp. 'thermophila' J18 A0A0H3U0Y7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme 2.7fold from Escherichia coli strain BL21 by nickel affinity chromatography Paecilomyces sp. 'thermophila'

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
24.2
-
purified recombinant enzyme, pH 7.5, 50°C, with NADH Paecilomyces sp. 'thermophila'
70.1
-
purified recombinant enzyme, pH 7.5, 50°C, with NADPH Paecilomyces sp. 'thermophila'

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycolate + NAD+
-
Paecilomyces sp. 'thermophila' glyoxylate + NADH + H+
-
?
glycolate + NAD+
-
Paecilomyces sp. 'thermophila' J18 glyoxylate + NADH + H+
-
?
glycolate + NADP+
-
Paecilomyces sp. 'thermophila' glyoxylate + NADPH + H+
-
?
glycolate + NADP+
-
Paecilomyces sp. 'thermophila' J18 glyoxylate + NADPH + H+
-
?
additional information the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate Paecilomyces sp. 'thermophila' ?
-
?
additional information the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate Paecilomyces sp. 'thermophila' J18 ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme Paecilomyces sp. 'thermophila'
More the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview Paecilomyces sp. 'thermophila'

Synonyms

Synonyms Comment Organism
glyoxylate reductase
-
Paecilomyces sp. 'thermophila'
PtGR
-
Paecilomyces sp. 'thermophila'

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Paecilomyces sp. 'thermophila'

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
recombinant enzyme, 1 h, 90% activity remaining Paecilomyces sp. 'thermophila'

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
at 30°C Paecilomyces sp. 'thermophila'

pH Stability

pH Stability pH Stability Maximum Comment Organism
4.5 10 recombinant enzyme, 30°C, 1 h, more than 80% of activity is retained Paecilomyces sp. 'thermophila'

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview Paecilomyces sp. 'thermophila'
NAD+
-
Paecilomyces sp. 'thermophila'
NADH
-
Paecilomyces sp. 'thermophila'
NADP+
-
Paecilomyces sp. 'thermophila'
NADPH
-
Paecilomyces sp. 'thermophila'

pI Value

Organism Comment pI Value Maximum pI Value
Paecilomyces sp. 'thermophila' sequence calculation
-
6.33

General Information

General Information Comment Organism
evolution the deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases Paecilomyces sp. 'thermophila'
metabolism glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism Paecilomyces sp. 'thermophila'