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
5.4.3.8
-
RECOMMENDED NAME
GeneOntology No.
glutamate-1-semialdehyde 2,1-aminomutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
-
-
-
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
intermolecular transamination occurs during conversion of (S)-4-amino-5-oxopentanoate to 5-amino-4-oxopentanoate
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
wild-type enzyme and gabaculine-resistant mutant enzyme use a ping-pong bi-bi mechanism in which 4,5-diaminovalerate is a likely intermediate
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
the catalytic mechanism includes enzyme-bound diaminovalerate as a central intermediate
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
ping-pong bi-bi mechanism in which 4,5-diaminovalerate is the second substrate and 4,5-dioxovalerate is an alternative first substrate
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
mechanism
-
L-glutamate 1-semialdehyde = 5-aminolevulinate
show the reaction diagram
enzyme shows an active-site gating loop, which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the other. Loop movement requires a beta-sheet-to-alpha-helix transition to assume the closed conformation, thus facilitating transport of substrate toward, and concomitantly forming, an integral part of the active site. The accompanying intersubunit cross-talk controls negative cooperativity between the allosteric pair
P24630
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, amino group
-
isomerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
tetrapyrrole biosynthesis I (from glutamate)
-
SYSTEMATIC NAME
IUBMB Comments
(S)-4-amino-5-oxopentanoate 4,5-aminomutase
Requires pyridoxal phosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Aminotransferase, glutamate semialdehyde
-
-
-
-
Glutamate 1-semialdehyde aminotransferase
-
-
-
-
glutamate-1-semialdehyde aminomutase
P30949
-
glutamate-1-semialdehyde aminomutase
P24630
-
Glutamate-1-semialdehyde aminotransferase
-
-
-
-
Glutamate-1-semialdehyde aminotransferase
P30949
-
Glutamate-1-semialdehyde aminotransferase
-
-
Glutamate-1-semialdehyde aminotransferase
Escherichia coli MG1655
-
-
-
GSA
-
-
-
-
GSA aminotransferase
-
-
-
-
GSA-AT
-
-
-
-
GSA-AT
P30949
-
GSA-AT
-
-
GSAM
P30949
-
GSAM
P24630
-
HemL
Escherichia coli MG1655
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
68518-07-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
wild-type and active site mutant K265R
-
-
Manually annotated by BRENDA team
Escherichia coli MG1655
-
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus 98-3
-
-
-
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
strain PCC 6301
UniProt
Manually annotated by BRENDA team
wild-type and mutant enzyme Lys272Ala
-
-
Manually annotated by BRENDA team
wild-type strain and gabaculine-resistant strain
-
-
Manually annotated by BRENDA team
pv. phaseoli
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
co-expression of hemL with hemAM achieves asignificantly increased 5-aminolevulinate production
physiological function
Escherichia coli MG1655
-
co-expression of hemL with hemAM achieves asignificantly increased 5-aminolevulinate production
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
-
-
-
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
show the reaction diagram
-
anomalous enantiomeric reaction with the (R)enantiomer
-
-
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
-
-
r
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
-
-
r
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
P24630
-
-
-
?
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
involved in chlorophyll biosynthesis
-
r
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
involved in conversion of glutamate to 5-aminolevulinate
-
r
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
-
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
induction of enzyme synthesis by light
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
key enzyme in plant tetrapyrrole synthesis
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
4,5-diaminovalerate may be an intermediate in the synthesis of 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
formation of 5-aminolevulinic acid, which is the first committed precursor of chlorophyll biosynthesis in the chloroplast
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
key enzyme in the synthetic pathway leading to chlorophyll
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
the enzyme may catalyze a part reaction in the conversion of L-Glu to 5-amino-4-oxopentanoate in greening plastids
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
-
-
-
4,5-Diaminovalerate
?
show the reaction diagram
-
is a substrate for the pyridoxal 5'-phosphate form of the enzyme
-
-
-
4,5-Diaminovalerate
?
show the reaction diagram
-
is a substrate for the pyridoxal 5'-phosphate form of the enzyme
-
-
-
4,5-Diaminovalerate
?
show the reaction diagram
-
is a substrate for the pyridoxal 5'-phosphate form of the enzyme
-
-
-
4,5-Dioxovalerate
5-Amino-4-oxopentanoate
show the reaction diagram
-
is a substrate for the pyridoxamine form of the enzyme
-
-
4,5-Dioxovalerate
5-Amino-4-oxopentanoate
show the reaction diagram
-
is a substrate for the pyridoxamine form of the enzyme
-
-
4,5-Dioxovalerate
5-Amino-4-oxopentanoate
show the reaction diagram
-
is a substrate for the pyridoxamine form of the enzyme
-
-
glutamate-1-semialdehyde
5-amino-levulinate
show the reaction diagram
Sulfolobus solfataricus, Sulfolobus solfataricus 98-3
-
the enzyme is involved in biosynthesis of the tetrapyrrole precursor, delta-aminolevulinic acid, from glutamate by the tRNA-dependent five-carbon pathway
-
-
?
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
-
-
-
-
?
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
-, P30949
-
-
-
?
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
Escherichia coli MG1655
-
-
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
involved in chlorophyll biosynthesis
-
r
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
show the reaction diagram
-
involved in conversion of glutamate to 5-aminolevulinate
-
r
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
-
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
induction of enzyme synthesis by light
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
key enzyme in plant tetrapyrrole synthesis
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
4,5-diaminovalerate may be an intermediate in the synthesis of 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
formation of 5-aminolevulinic acid, which is the first committed precursor of chlorophyll biosynthesis in the chloroplast
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
key enzyme in the synthetic pathway leading to chlorophyll
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
the enzyme may catalyze a part reaction in the conversion of L-Glu to 5-amino-4-oxopentanoate in greening plastids
-
-
-
(S)-4-Amino-5-oxopentanoate
?
show the reaction diagram
-
4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates
-
-
-
glutamate-1-semialdehyde
5-amino-levulinate
show the reaction diagram
Sulfolobus solfataricus, Sulfolobus solfataricus 98-3
-
the enzyme is involved in biosynthesis of the tetrapyrrole precursor, delta-aminolevulinic acid, from glutamate by the tRNA-dependent five-carbon pathway
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
cofactor is bound by a Schiff base to the protein
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
acts as cofactor and stimulates
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binding site
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
P24630
dependent on
pyridoxal 5'-phosphate
-, P30949
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxamine 5'-phosphate
-
stimulates
pyridoxamine 5'-phosphate
-
only the pyridoxamine form of the enzyme is active
pyridoxamine 5'-phosphate
-
cofactor
pyridoxamine 5'-phosphate
-
the pyridoxal-phosphate form of the enzyme and the pyridoxamine-phosphate form of the enzyme are similarly active
pyridoxamine 5'-phosphate
-
conversion into the active pyridoxamine-phosphate form of enzyme in an exponential process
pyridoxamine 5'-phosphate
P24630
dependent on
pyridoxamine 5'-phosphate
-, P30949
dependent on
vitamin B6
-
wild-type enzyme and gabaculine-resistant mutant enzyme contain vitamin B6
vitamin B6
-
subunits show asymmetry in cofactor binding
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
15 mM Mg2+ has no effect on activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,5-Dioxovalerate
-
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
-
-
4-Amino-5-hexenoic acid
-
-
4-Amino-5-hexynoic acid
-
-
Aminooxyacetate
-
20 mM, 57% inhibition
Cycloserine
-
20 mM, 43% inhibition
D-penicillamine
-
20 mM, 9% inhibition
gabaculine
-
0.005 mM, 83% inhibition. Irreversible inhibition which requires the presence of either glutamate-1-semialdehyde or 5-amino-4-oxopentanoate
gabaculine
-
complete inactivation by gabaculine when the enzyme is exposed to 5-amino-4-oxopentanoate, levulinate or 4,5-dioxovalerate in absence of glutamate 1-semialdehyde
gabaculine
-
0.0005 mM, 50% inhibition. The inhibition is reversible up to 1 h after its addition, if the gabaculine is removed by gel filtration, before the enzyme is incubated by gel filtration, before the enzyme is incubated with substrate. Irreversible inhibition is obtained by preincubation of the enzyme at 30C either for several hours with gabaculine alone or for a few min with both gabaculine and glutamate-1-semialdehyde
gabaculine
-
wild-type enzyme is inhibited, gabaculine-resistant mutant enzyme is not inhibited
gabaculine
P24630
potent inhibitor
p-chloromercuribenzoate
-
0.1 mM, 45% inhibition
pyridoxal 5'-phosphate
-
5 mM, 47% inhibition
pyridoxal 5'-phosphate
-
-
glyoxylate
-
20 mM, 27% inhibition
additional information
-
no inhibition by 3-hydroxyglutamate
-
additional information
-
5 mM EDTA has no effect on activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ethanolamine
-
stimulates activity of mutant enzyme Lys265Arg
glutamate
-
3fold activation of tagless recombinant enzyme
Methylamine
-
stimulates activity of mutant enzyme Lys265Arg
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.022
-
(S)-4-Amino-5-oxopentanoate
-
gabaculine-resistant mutant enzyme
0.025
-
(S)-4-Amino-5-oxopentanoate
-
-
0.046
-
(S)-4-Amino-5-oxopentanoate
-
wild-type enzyme
0.067
-
(S)-4-Amino-5-oxopentanoate
-
-
0.38
-
(S)-4-Amino-5-oxopentanoate
-
-
0.4
-
(S)-4-Amino-5-oxopentanoate
-
-
0.001
-
4,5-Diaminovalerate
-
-
1.4
-
4,5-Dioxovalerate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.077
-
(S)-4-Amino-5-oxopentanoate
-
gabaculine-resistant mutant enzyme
0.11
-
(S)-4-Amino-5-oxopentanoate
-
-
0.47
-
(S)-4-Amino-5-oxopentanoate
-
wild-type enzyme
0.95
-
(S)-4-Amino-5-oxopentanoate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0028
-
gabaculine
P24630
wild type enzyme
0.32
-
gabaculine
P24630
mutant enzyme M248I
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00009
-
-
-
0.0022
-
P24630
mutant enzyme M248I
0.0123
-
P24630
wild type enzyme
0.015
-
-
recombinant GSA-AT
0.384
-
-
-
1.4
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
broad
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8
-
pH 6.5: about 30% of maximal activity, pH 8.0: about 50% of maximal activity
6.7
8.8
-
pH 6.7: about 45% of maximal activity, pH 8.8: about 90% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14
30
-
14C: 41% of maximal activity, 22C: 76.4% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
low specific activity in etiolated plastids compared to greening plastids
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
-
-
gel filtration
43000
-
-
gel filtration, nondenaturing rate zonal sedimentation on glycerol gradients
87000
-
-
gel filtration
88000
-
-
native and recombinant GSA-AT, gel filtration
98000
-
-
gel filtration
100000
-
-
gel filtration
500000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 67000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 45932, calculation from nucleotide sequence
?
-
x * 45043, calculation from nucleotide sequence
dimer
-
2 * 46000, SDS-PAGE; 2 * 46172, calculation from nucleotide sequence
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 45500, SDS-PAGE, native and recombinant GSA-AT
homodimer
-, P30949
x-ray crystallography
monomer
-
1 * 43000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, P30949
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
P24630
wild-type and mutant enzyme Lys272Ala
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nickel-chelating resin column chromatography and Superdex 200 gel filtration
-, P30949
recombinant enzyme
-
recombinant GSA-AT
-
partial
-
recombinant enzyme
-
recombinant GSAT
-
wild-type enzyme and gabaculine-resistant mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-, P30949
expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli DEX cells
-
mutant enzyme Lys265Arg, overexpression
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli
P24630
expression in Escherichia coli
-
wild-type enzyme and gabaculine-resistant mutant enzyme, overexpression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression of gltX does not affect the transcription of hemL
-
overexpression of gltX does not affect the transcription of hemL
Escherichia coli MG1655
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L265E
-
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
-
mutant enzyme Lys272Ala is inactive
M248I
P24630
the M248I point mutation confers about 100fold increased gabaculine resistance to GSAM
additional information
-
gabaculine-resistant mutant enzyme with a 3 times lower catalytic efficiency and impaired prototropic rearrangement and transaldimination