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

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
5.4.3.8
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RECOMMENDED NAME
GeneOntology No.
glutamate-1-semialdehyde 2,1-aminomutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular, amino group
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isomerization
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heme metabolism
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Metabolic pathways
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Porphyrin and chlorophyll metabolism
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tetrapyrrole biosynthesis I (from glutamate)
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SYSTEMATIC NAME
IUBMB Comments
(S)-4-amino-5-oxopentanoate 4,5-aminomutase
Requires pyridoxal phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
68518-07-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
pv. phaseoli
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
the entrance of the catalytic site is protected by a loop that is believed to switch from an open to a closed conformation during catalysis. The structure of the mobile loop is related to the form of the cofactor bound to the active site, allowing for asymmetry within the dimer the structure of the mobile loop is related to the form of the cofactor bound to the active site, allowing for asymmetry within the dimer. Conformation of the active site loop in different crystal forms of dimeric and active site accessibility, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
4,5-Diaminovalerate
?
show the reaction diagram
4,5-Dioxovalerate
5-Amino-4-oxopentanoate
show the reaction diagram
glutamate-1-semialdehyde
5-amino-levulinate
show the reaction diagram
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
additional information
?
-
-
complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis suggests direct metabolic channeling between both enzymes to protect the reactive aldehyde species glutamate-1-semialdehyde
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
glutamate-1-semialdehyde
5-amino-levulinate
show the reaction diagram
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
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-
-
-
?
additional information
?
-
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complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis suggests direct metabolic channeling between both enzymes to protect the reactive aldehyde species glutamate-1-semialdehyde
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
vitamin B6
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,5-Dioxovalerate
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competitive inhibition of pyridoxamine-phosphate form of the enzyme and mixed-type inhibition of the pyridoxal-phosphate form of the enzyme
4-Amino-5-fluoro-pentanoic acid
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4-Amino-5-hexenoic acid
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4-Amino-5-hexynoic acid
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Aminooxyacetate
cycloserine
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20 mM, 43% inhibition
D-penicillamine
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20 mM, 9% inhibition
gabaculine
glyoxylate
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20 mM, 27% inhibition
p-chloromercuribenzoate
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0.1 mM, 45% inhibition
pyridoxal 5'-phosphate
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanolamine
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stimulates activity of mutant enzyme Lys265Arg
glutamate
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3fold activation of tagless recombinant enzyme
methylamine
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stimulates activity of mutant enzyme Lys265Arg
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 0.4
(S)-4-Amino-5-oxopentanoate
0.001
4,5-Diaminovalerate
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1.4
4,5-Dioxovalerate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077 - 0.95
(S)-4-Amino-5-oxopentanoate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 0.32
gabaculine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00009
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-
0.0022
mutant enzyme M248I
0.0123
wild type enzyme
0.015
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recombinant GSA-AT
0.384
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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broad
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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pH 6.5: about 30% of maximal activity, pH 8.0: about 50% of maximal activity
6.7 - 8.8
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pH 6.7: about 45% of maximal activity, pH 8.8: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14 - 30
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14C: 41% of maximal activity, 22C: 76.4% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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low specific activity in etiolated plastids compared to greening plastids
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Bacillus subtilis (strain 168)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Synechococcus elongatus (strain PCC 7942)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Thermosynechococcus elongatus (strain BP-1)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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gel filtration
43000
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gel filtration, nondenaturing rate zonal sedimentation on glycerol gradients
87000
gel filtration
88000
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native and recombinant GSA-AT, gel filtration
98000
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gel filtration
100000
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gel filtration
500000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
monomer
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1 * 43000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with pyridoxamine 5'-phosphate, hanging drop vapor diffusion method, using 0.1 M Bicine pH 8.5, 30% (w/v) PEG 3350, at 23C
wild type enzyme and mutant enzyme M248I are crystallized by the vapor diffusion method, using 11.5% (w/v) PEG 8.000 and 150 mM magnesium acetate, pH 6.8
wild-type and mutant enzyme Lys272Ala
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-chelating resin column chromatography and Superdex 200 gel filtration
partial
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recombinant enzyme
recombinant GSA-AT
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recombinant GSAT
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wild-type enzyme and gabaculine-resistant mutant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DEX cells
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expression in Escherichia coli
mutant enzyme Lys265Arg, overexpression
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wild-type enzyme and gabaculine-resistant mutant enzyme, overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpression of gltX does not affect the transcription of hemL
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
K272A
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mutant enzyme Lys272Ala is inactive
M248I
the M248I point mutation confers about 100fold increased gabaculine resistance to GSAM
additional information
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gabaculine-resistant mutant enzyme with a 3 times lower catalytic efficiency and impaired prototropic rearrangement and transaldimination
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