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.

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

     5 Isomerases

         5.4 Intramolecular transferases

             5.4.3 Transferring amino groups

                5.4.3.8 glutamate-1-semialdehyde 2,1-aminomutase

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Results	in table
3	Activating Compound
32180	AA Sequence
1	CAS Registry Number
17	Cloned(Commentary)
25	Cofactor
8	Crystallization (Commentary)
2	Expression
8	General Information
2	IC50 Value
23	Inhibitors
8	KM Value [mM]
5	Localization
2	Metals/Ions
17	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
74	Organism
7	Pathway
50	PDB ID
3	pH Optimum
2	pH Range
8	Protein Variants
16	Purification (Commentary)
8	Reaction
2	Reaction Type
47	Reference
7	Source Tissue
8	Specific Activity [micromol/min/mg]
68	Substrates and Products (Substrate)
19	Subunits
39	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Turnover Number [1/s]

Engineering

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Engineering on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

L265E

Escherichia coli

-

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

3432

K286A

2 entries

K272A

Synechococcus sp.

-

mutant enzyme Lys272Ala is inactive

3421

M248I

Synechococcus sp.

P24630

the M248I point mutation confers about 100fold increased gabaculine resistance to GSAM

703619

additional information

3 entries

K286A

Pseudomonas aeruginosa

Q9HWU0

site-directed mutagenesis

747005

K286A

Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1

-

site-directed mutagenesis

-

additional information

Corynebacterium glutamicum

Q8NT73

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

747678

additional information

Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025

-

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

Synechococcus sp.

-

gabaculine-resistant mutant enzyme with a 3 times lower catalytic efficiency and impaired prototropic rearrangement and transaldimination

3430