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Literature summary extracted from

  • Kuivanen, J.; Arvas, M.; Richard, P.
    Clustered genes encoding 2-keto-L-gulonate reductase and L-idonate 5-dehydrogenase in the novel fungal D-glucuronic acid pathway (2017), Front. Microbiol., 8, 225 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.215 gene gluD, clustered with gene gluE, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains ATCC 90845 and modified CEN.PK2, subcloning in Escherichia coli strain TOP10 Aspergillus niger
1.1.1.264 expression in Escherichia coli TOP10 cells Aspergillus niger
1.1.1.264 expression in Saccharomyces cerevisiae Aspergillus niger
1.1.1.366 gene gluE, clustered with gene gluD, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strains ATCC 90845 and modified CEN.PK2, subcloning in Escherichia coli strain TOP10 Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.215 additional information identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluD deletion mutant strain, phenotype, overview. Deletion of gluD does not result in reduced or no growth on D-glcUA as sole carbon source, but it results in a phenotype of accumulating 2-keto-L-gulonate when cultivating on D-glcUA Aspergillus niger
1.1.1.366 additional information identification of a gene cluster encoding NADPH-dependent, L-idonate forming, 2-keto-L-gulonate reductase and NAD+-dependent L-idonate 5-dehydrogenase which forms 5-keto-D-gluconate. These genes are involved in the fungal D-glcUA catabolism and the reaction catalyzed by the latter enzyme is a direct continuation for the previously identified reaction by the action of GluC. Generation of a gene gluE deletion mutant strain, phenotype, overview. The gluE deletion in Aspergillus niger causes a phenotype with reduced growth and ceased D-glcUA consumption Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.215 12.6
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.215 25.3
-
2-oxo-L-gulonate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.264 8.4
-
5-Dehydro-D-gluconate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.264 8.4
-
5-Dehydro-D-gluconate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.264 30.9
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.264 30.9
-
L-Idonate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.366 8.4
-
5-Dehydro-D-gluconate pH 8.0, temperature not specified in the publication Aspergillus niger
1.1.1.366 30.9
-
L-Idonate pH 7.0, temperature not specified in the publication Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.264 L-idonate + NAD+ Aspergillus niger the enzyme is part of the D-glucuronic acid catabolism 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ Aspergillus niger ATCC 1015 the enzyme is part of the D-glucuronic acid catabolism 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ Aspergillus niger CBS 113.46 the enzyme is part of the D-glucuronic acid catabolism 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.366 5-dehydro-D-gluconate + NADH + H+ Aspergillus niger
-
L-idonate + NAD+
-
r
1.1.1.366 L-idonate + NAD+ Aspergillus niger
-
5-dehydro-D-gluconate + NADH + H+
-
r
1.1.1.366 L-idonate + NAD+ Aspergillus niger ATCC 1015
-
5-dehydro-D-gluconate + NADH + H+
-
r
1.1.1.366 L-idonate + NAD+ Aspergillus niger CBS 113.46
-
5-dehydro-D-gluconate + NADH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.215 Aspergillus niger A0A1D8RK43
-
-
1.1.1.215 Aspergillus niger ATCC 1015 A0A1D8RK43
-
-
1.1.1.215 Aspergillus niger CBS 113.46 A0A1D8RK43
-
-
1.1.1.264 Aspergillus niger
-
-
-
1.1.1.264 Aspergillus niger ATCC 1015
-
-
-
1.1.1.366 Aspergillus niger
-
-
-
1.1.1.366 Aspergillus niger ATCC 1015
-
-
-
1.1.1.366 Aspergillus niger CBS 113.46
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.264
-
Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.215 2-oxo-L-gulonate + NADPH + H+
-
Aspergillus niger L-idonate + NADP+
-
r
1.1.1.215 2-oxo-L-gulonate + NADPH + H+
-
Aspergillus niger ATCC 1015 L-idonate + NADP+
-
r
1.1.1.215 2-oxo-L-gulonate + NADPH + H+
-
Aspergillus niger CBS 113.46 L-idonate + NADP+
-
r
1.1.1.215 L-idonate + NADP+
-
Aspergillus niger 2-oxo-L-gulonate + NADPH + H+
-
r
1.1.1.215 L-idonate + NADP+
-
Aspergillus niger ATCC 1015 2-oxo-L-gulonate + NADPH + H+
-
r
1.1.1.215 L-idonate + NADP+
-
Aspergillus niger CBS 113.46 2-oxo-L-gulonate + NADPH + H+
-
r
1.1.1.264 5-dehydro-D-gluconate + NADH + H+
-
Aspergillus niger L-idonate + NAD+
-
?
1.1.1.264 5-dehydro-D-gluconate + NADH + H+
-
Aspergillus niger ATCC 1015 L-idonate + NAD+
-
?
1.1.1.264 5-dehydro-D-gluconate + NADH + H+
-
Aspergillus niger CBS 113.46 L-idonate + NAD+
-
?
1.1.1.264 L-idonate + NAD+
-
Aspergillus niger 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme is part of the D-glucuronic acid catabolism Aspergillus niger 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme has a strict requirement for NAD+/NADH Aspergillus niger 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+
-
Aspergillus niger ATCC 1015 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme is part of the D-glucuronic acid catabolism Aspergillus niger ATCC 1015 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme has a strict requirement for NAD+/NADH Aspergillus niger ATCC 1015 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+
-
Aspergillus niger CBS 113.46 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme is part of the D-glucuronic acid catabolism Aspergillus niger CBS 113.46 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.264 L-idonate + NAD+ the enzyme has a strict requirement for NAD+/NADH Aspergillus niger CBS 113.46 5-dehydro-D-gluconate + NADH + H+
-
?
1.1.1.366 5-dehydro-D-gluconate + NADH + H+
-
Aspergillus niger L-idonate + NAD+
-
r
1.1.1.366 L-idonate + NAD+
-
Aspergillus niger 5-dehydro-D-gluconate + NADH + H+
-
r
1.1.1.366 L-idonate + NAD+
-
Aspergillus niger ATCC 1015 5-dehydro-D-gluconate + NADH + H+
-
r
1.1.1.366 L-idonate + NAD+
-
Aspergillus niger CBS 113.46 5-dehydro-D-gluconate + NADH + H+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.215 2-keto-L-gulonate reductase
-
Aspergillus niger
1.1.1.215 GluD
-
Aspergillus niger
1.1.1.215 NADPH requiring 2-keto-L-gulonate reductase
-
Aspergillus niger
1.1.1.264 GluE
-
Aspergillus niger
1.1.1.366 GluE
-
Aspergillus niger
1.1.1.366 L-idonate 5-dehydrogenase
-
Aspergillus niger
1.1.1.366 NAD+ requiring L-idonate 5-dehydrogenase
-
Aspergillus niger

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.215 1.1
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.215 21.4
-
2-oxo-L-gulonate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.264 5.5
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.264 5.5
-
L-Idonate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.264 7.2
-
5-Dehydro-D-gluconate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.264 7.2
-
5-Dehydro-D-gluconate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.366 5.5
-
L-Idonate pH 7.0, temperature not specified in the publication Aspergillus niger
1.1.1.366 7.2
-
5-Dehydro-D-gluconate pH 8.0, temperature not specified in the publication Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.215 7
-
assay at, L-idonate oxidation Aspergillus niger
1.1.1.366 7
-
assay at, L-idonate oxidation Aspergillus niger
1.1.1.366 8
-
assay at, 5-dehydro-D-gluconate reduction Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.215 NADP+ strict requirement for NADP+/NADPH as cofactors Aspergillus niger
1.1.1.215 NADPH strict requirement for NADP+/NADPH as cofactors Aspergillus niger
1.1.1.264 NAD+ strict requirement for NAD+/NADH as cofactors Aspergillus niger
1.1.1.264 NAD+ the enzyme has a strict requirement for NAD+/NADH Aspergillus niger
1.1.1.264 NADH strict requirement for NAD+/NADH as cofactors Aspergillus niger
1.1.1.264 NADH the enzyme has a strict requirement for NAD+/NADH Aspergillus niger
1.1.1.366 NAD+ GluE has a strict requirement for NAD+/NADH as cofactors Aspergillus niger
1.1.1.366 NADH GluE has a strict requirement for NAD+/NADH as cofactors Aspergillus niger

General Information

EC Number General Information Comment Organism
1.1.1.215 malfunction gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism Aspergillus niger
1.1.1.215 metabolism in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD. The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE (EC 1.1.1.366). The genes coding for these two enzymes are clustered and share the same bidirectional promoter Aspergillus niger
1.1.1.215 physiological function a GluD deletion mutant does not show reduced growth when cultivated on agar plate with D-glucuronate as sole carbon source. In the liquid cultivation on D-glucuronate, 2-oxo-L-gulonate accumulates in the medium after D-glucuronate is consumed Aspergillus niger
1.1.1.264 metabolism the enzyme is part of the D-glucuronic acid catabolism Aspergillus niger
1.1.1.264 physiological function GluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism Aspergillus niger
1.1.1.366 malfunction gluD deletion results in accumulation of 2-keto-L-gulonate in the liquid cultivation, while the gluE deletion results in reduced growth and cessation of the D-glucuronic acid catabolism Aspergillus niger
1.1.1.366 metabolism in the filamentous fungus Aspergillus niger, the enzymes that are known to be part of the D-glucuronic acid catabolism pathway are the NADPH requiring D-glucuronic acid reductase forming L-gulonate and the NADH requiring 2-keto-L-gulonate reductase that forms L-idonate. With the aid of RNA sequencing two more enzymes of the pathway are identified. The first is a NADPH requiring 2-keto-L-gulonate reductase that forms L-idonate, GluD (EC 1.1.1.264). The second is a NAD+ requiring L-idonate 5-dehydrogenase forming 5-keto-gluconate, GluE. The genes coding for these two enzymes are clustered and share the same bidirectional promoter Aspergillus niger

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.215 0.087
-
L-Idonate pH 7.0, temperature not specified in the publication Aspergillus niger
1.1.1.215 0.087
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.215 0.846
-
2-oxo-L-gulonate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.215 0.85
-
2-dehydro-D-gluconate pH 8.0, temperature not specified in the publication Aspergillus niger
1.1.1.264 0.178
-
L-Idonate pH 8, temperature not specified in the publication Aspergillus niger
1.1.1.264 0.857
-
5-Dehydro-D-gluconate pH 7, temperature not specified in the publication Aspergillus niger
1.1.1.366 0.18
-
L-Idonate pH 7.0, temperature not specified in the publication Aspergillus niger
1.1.1.366 0.86
-
5-Dehydro-D-gluconate pH 8.0, temperature not specified in the publication Aspergillus niger