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Literature summary for 1.4.1.4 extracted from

  • Trotter, P.J.; Juco, K.; Le, H.T.; Nelson, K.; Tamayo, L.I.; Nicaud, J.M.; Park, Y.K.
    Glutamate dehydrogenases in the oleaginous yeast Yarrowia lipolytica (2020), Yeast, 37, 103-115 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in GDH-deficient Saccharomyces cerevisiae Yarrowia lipolytica
gene YALI0F17820g, cloned from strain INAG34815, sequence comparisons, recombinant expression in gdh-null Saccharomyces cerevisiae, recombinant overexpression in Yarrowia lipolytica strain under control of the constitutive TEF promoter using the JMP62 expression vectors. GDH activities in Yarrowia lipolytica are differentially expressed, overview Yarrowia lipolytica

Protein Variants

Protein Variants Comment Organism
additional information YALI0F17820g gene deletion followed by growth on different carbon and nitrogen sources, and enzyme overvexpression. Disruption of ylGDH1 and ylGDH2 (gdh1DELTA gdh2DELTA) completely abolishes both NADP- and NAD-GDH activities Yarrowia lipolytica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + H2O + NADP+ Yarrowia lipolytica
-
2-oxoglutarate + NH3 + NADPH + H+
-
r
L-glutamate + H2O + NADP+ Yarrowia lipolytica CLIB 122
-
2-oxoglutarate + NH3 + NADPH + H+
-
r
L-glutamate + H2O + NADP+ Yarrowia lipolytica E 150
-
2-oxoglutarate + NH3 + NADPH + H+
-
r

Organism

Organism UniProt Comment Textmining
Yarrowia lipolytica Q6C1A9
-
-
Yarrowia lipolytica Q6C1A9 isoform GDH1
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Yarrowia lipolytica CLIB 122 Q6C1A9
-
-
Yarrowia lipolytica CLIB 122 Q6C1A9 isoform GDH1
-
Yarrowia lipolytica E 150 Q6C1A9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells Yarrowia lipolytica
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + NH3 + NADPH + H+
-
Yarrowia lipolytica L-glutamate + H2O + NADP+
-
?
2-oxoglutarate + NH3 + NADPH + H+
-
Yarrowia lipolytica CLIB 122 L-glutamate + H2O + NADP+
-
?
2-oxoglutarate + NH3 + NADPH + H+
-
Yarrowia lipolytica E 150 L-glutamate + H2O + NADP+
-
?
L-glutamate + H2O + NADP+
-
Yarrowia lipolytica 2-oxoglutarate + NH3 + NADPH + H+
-
r
L-glutamate + H2O + NADP+
-
Yarrowia lipolytica CLIB 122 2-oxoglutarate + NH3 + NADPH + H+
-
r
L-glutamate + H2O + NADP+
-
Yarrowia lipolytica E 150 2-oxoglutarate + NH3 + NADPH + H+
-
r

Synonyms

Synonyms Comment Organism
NADP-dependent GDH
-
Yarrowia lipolytica
NADP-ylGdh1p
-
Yarrowia lipolytica
YALI0F17820g
-
Yarrowia lipolytica
ylGDH1
-
Yarrowia lipolytica

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Yarrowia lipolytica
NADPH
-
Yarrowia lipolytica

Expression

Organism Comment Expression
Yarrowia lipolytica replacement of ammonia with glutamate in growth medium causes a decrease in NADP-ylGdh1p activity down
Yarrowia lipolytica during logarithmic growth on rich medium, the NADP-ylGDH1p enzyme activity is most highly expressed and induced in stationary and nitrogen starved cells by 3fold to 12fold up

General Information

General Information Comment Organism
metabolism YALI0F17820g (ylGDH, EC 1.4.1.4) encodes a NADP-dependent GDH whereas YALI0E09603g (ylGDH2, EC 1.4.1.2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. Levels of the two enzyme activities are comparable during logarithmic growth on rich medium, but the NADP-ylGDH1p enzyme activity is most highly expressed in stationary and nitrogen starved cells by 3fold to 12fold compared to NAD-ylGDH2p. Replacement of ammonia with glutamate causes a decrease in NADP-ylGdh1p activity, whereas NAD-ylGdh2p activity is increased. When glutamate is both carbon and nitrogen sources, the activity of NAD-ylGDH2p becomes dominant up to 18fold compared with that of NADP-ylGDH1p. ylGDH1 and ylGDH2 are functionally not interchangeable Yarrowia lipolytica
physiological function gene YALI0F17820g (GDH1) encodes a NADP?dependent GDH whereas YALI0E09603g (GDH2) encodes a NAD-dependent GDH enzyme. The activity encoded by these two genes accounts for all measurable GDH activity in Yarrowia lipolytica. NADP-GDH1 enzyme activity is most highly expressed in stationary and nitrogen starved cells. NADP-Gdh1 is required for efficient nitrogen assimilation. GDH1 and GDH2 are not interchangeable Yarrowia lipolytica
physiological function glutamate dehydrogenases (GDHs) are fundamental to cellular nitrogen and energy balance. NADP-ylGdh1p is required for efficient nitrogen assimilation. Glutamate dehydrogenase (GDH) activity in gdh-null Saccharomyces cerevisiae mutant cells is restored by introduction of YALI0F17820g (ylGDH1) or YALI0E09603g (ylGDH2, EC 1.4.1.2) from Yarrowia lipolytica Yarrowia lipolytica