5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase
This is an abbreviated version!
For detailed information about glutamate-1-semialdehyde 2,1-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.8
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5.4.3.8
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chlorophyll
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5-aminolevulinic
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tetrapyrrole
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glutamyl-trna
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delta-aminolevulinic
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synechococcus
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gabaculine
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hema
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4,5-diaminovalerate
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trnaglu
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4,5-dioxovalerate
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aldimine
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glutr
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five-carbon
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glutamyl-trnaglu
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trna-dependent
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3-amino-2,3-dihydrobenzoic
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chelatase
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mg-chelatase
- 5.4.3.8
- chlorophyll
-
5-aminolevulinic
- tetrapyrrole
- glutamyl-trna
-
delta-aminolevulinic
- synechococcus
- gabaculine
- hema
- 4,5-diaminovalerate
- trnaglu
- 4,5-dioxovalerate
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aldimine
- glutr
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five-carbon
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glutamyl-trnaglu
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trna-dependent
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3-amino-2,3-dihydrobenzoic
- chelatase
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mg-chelatase
Reaction
Synonyms
Aminotransferase, glutamate semialdehyde, AtGSA1, EC 2.7.2.13, Glutamate 1-semialdehyde aminotransferase, glutamate-1-semialdehyde amino-transferase, glutamate-1-semialdehyde aminomutase, Glutamate-1-semialdehyde aminotransferase, glutamate-1-semialdehyde-2,1-aminomutase, glutamate-1-semialdehyde-aminomutase, GSA, GSA aminotransferase, GSA-AT, GSA1, GSAM, GSAT, HemL, PA4088, protein PA4088
ECTree
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Engineering
Engineering on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase
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L265E
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mutant Lys265Arg has 2% of the enzymatic activity compared to the wild-type enzyme, the dimeric structure is not influenced, activity is stimulated by addition of exogenous amines such as ethanolamine and methylamine
K286A
M248I
the M248I point mutation confers about 100fold increased gabaculine resistance to GSAM
additional information
K286A
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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site-directed mutagenesis
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improved biological production of 5-aminolevulinate in Corynebacterium glutamicum is achieved by overexpressing the glutamate-initiated C5 pathway. Copies of the glutamyl t-RNA reductase HemA from several bacteria (Corynebacterium glutamicum, Escherichia coli, Bacillus subtilis, Salmonella typhimurium, and Klebsiella pneumoniae) are mutated by site-directed mutagenesis of which a HemA version from Salmonella typhimurium exhibits the highest 5-aminolevulinate production. Cultivation of the HemA-expressing strain produces approximately 204 mg/l of 5-aminolevulinate, while co-expression with HemL (glutamate-1-semialdehyde amino-transferase) increases 5-aminolevulinate concentration to 457 mg/L, representing 11.6fold and 25.9fold increases over the control strain (17 mg/l of 5-aminolevulinate). 5-Aminolevulinate overproduction can also be increased by reducing the formation of heme, which has been shown to have inhibitory effects on HemA activity. Method evaluation and optimization, overview
additional information
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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improved biological production of 5-aminolevulinate in Corynebacterium glutamicum is achieved by overexpressing the glutamate-initiated C5 pathway. Copies of the glutamyl t-RNA reductase HemA from several bacteria (Corynebacterium glutamicum, Escherichia coli, Bacillus subtilis, Salmonella typhimurium, and Klebsiella pneumoniae) are mutated by site-directed mutagenesis of which a HemA version from Salmonella typhimurium exhibits the highest 5-aminolevulinate production. Cultivation of the HemA-expressing strain produces approximately 204 mg/l of 5-aminolevulinate, while co-expression with HemL (glutamate-1-semialdehyde amino-transferase) increases 5-aminolevulinate concentration to 457 mg/L, representing 11.6fold and 25.9fold increases over the control strain (17 mg/l of 5-aminolevulinate). 5-Aminolevulinate overproduction can also be increased by reducing the formation of heme, which has been shown to have inhibitory effects on HemA activity. Method evaluation and optimization, overview
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additional information
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gabaculine-resistant mutant enzyme with a 3 times lower catalytic efficiency and impaired prototropic rearrangement and transaldimination