BRENDA - Enzyme Database

New insights in the topology of the biosynthesis of 5-aminolevulinic acid

Czarnecki, O.; Grimm, B.; Plant Signal. Behav. 8, e23124 (2013)

Data extracted from this reference:

Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.2.1.70
chloroplast
spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms delta-aminolevulinic acid (ALA) starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP)
Arabidopsis thaliana
9507
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.70
Arabidopsis thaliana
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.2.1.70
seedling
-
Arabidopsis thaliana
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743544
Arabidopsis thaliana
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADP+
-
Arabidopsis thaliana
1.2.1.70
NADPH
-
Arabidopsis thaliana
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.70
NADP+
-
Arabidopsis thaliana
1.2.1.70
NADPH
-
Arabidopsis thaliana
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.2.1.70
chloroplast
spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms delta-aminolevulinic acid (ALA) starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP)
Arabidopsis thaliana
9507
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
Arabidopsis thaliana
-
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.2.1.70
seedling
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.70
L-glutamyl-tRNAGlu + NADPH + H+
-
743544
Arabidopsis thaliana
L-glutamate 1-semialdehyde + NADP+ + tRNAGlu
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
1.2.1.70
metabolism
the enzyme is the first committed enzyme in tetrapyrrole biosynthesis reducing the activated tRNA-bound glutamate to glutamate-1-semialdehyde, which is subsequently transaminated by glutamate-1-semialdehyde aminotransferase (GSAT) to form 5-aminolevulinic acid. 5-Aminolevulinic acid formation is the rate limiting step of tetrapyrrole biosynthesis and temporally controlled by GluTR expression
Arabidopsis thaliana
1.2.1.70
physiological function
the enzyme is required for the biosynthesis of 5-aminolevulinic acid. Formation of 5-aminolevulinic acid at the beginning of the pathway is the rate limiting step of tetrapyrrole biosynthesis and target of multiple timely and spatially organized control mechanisms. Regulation of the pathway, detailed overview. Spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms 5-aminolevulinic acid starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP). At night the FLU protein, another glutamyl-tRNA reductase binding protein, binds the soluble glutamyl-tRNA reductase fraction to the thylakoid membrane and thereby inactivates 5-aminolevulinic acid formation. Only the GluTRBP bound fraction of GluTR can continue to synthesize 5-aminolevulinic acid during dark periods, preventing both a lack of heme during darkness and excessive accumulation of phototoxic intermediates of chlorophyll biosynthesis. The FLU protein i a negative regulator of 5-aminolevulinic acid biosynthesis
Arabidopsis thaliana
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.1.70
metabolism
the enzyme is the first committed enzyme in tetrapyrrole biosynthesis reducing the activated tRNA-bound glutamate to glutamate-1-semialdehyde, which is subsequently transaminated by glutamate-1-semialdehyde aminotransferase (GSAT) to form 5-aminolevulinic acid. 5-Aminolevulinic acid formation is the rate limiting step of tetrapyrrole biosynthesis and temporally controlled by GluTR expression
Arabidopsis thaliana
1.2.1.70
physiological function
the enzyme is required for the biosynthesis of 5-aminolevulinic acid. Formation of 5-aminolevulinic acid at the beginning of the pathway is the rate limiting step of tetrapyrrole biosynthesis and target of multiple timely and spatially organized control mechanisms. Regulation of the pathway, detailed overview. Spatial organization of 5-aminolevulinic acid formation in chloroplasts. The majority of a glutamyl-tRNA reductase (GluTR) and glutamate-1 semialdehyde aminotransferase (GSAT) protein complex is located in the stroma and forms 5-aminolevulinic acid starting with glutamyltRNAGlu, while a minor part of the active protein complex is attached to the thylakoid membrane via a GluTR-binding protein (GluTRBP). At night the FLU protein, another glutamyl-tRNA reductase binding protein, binds the soluble glutamyl-tRNA reductase fraction to the thylakoid membrane and thereby inactivates 5-aminolevulinic acid formation. Only the GluTRBP bound fraction of GluTR can continue to synthesize 5-aminolevulinic acid during dark periods, preventing both a lack of heme during darkness and excessive accumulation of phototoxic intermediates of chlorophyll biosynthesis. The FLU protein i a negative regulator of 5-aminolevulinic acid biosynthesis
Arabidopsis thaliana