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Information on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase and Organism(s) Synechococcus sp. and UniProt Accession P24630
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5.4.3.8 glutamate-1-semialdehyde 2,1-aminomutaseIUBMB Comments
Requires pyridoxal phosphate.
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Word Map
- 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
The taxonomic range for the selected organisms is: Synechococcus sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glutamate 1-semialdehyde aminotransferase, gsa-at, gsa aminotransferase, glutamate-1-semialdehyde aminotransferase, glutamate-1-semialdehyde aminomutase, glutamate-1-semialdehyde 2,1-aminomutase, glutamate-1-semialdehyde-2,1-aminomutase, atgsa1, pa4088, glutamate-1-semialdehyde amino-transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aminotransferase, glutamate semialdehyde
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Glutamate 1-semialdehyde aminotransferase
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Glutamate-1-semialdehyde aminotransferase
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GSA
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GSA aminotransferase
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GSA-AT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate 1-semialdehyde = 5-aminolevulinate
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
L-glutamate 1-semialdehyde = 5-aminolevulinate
ping-pong bi-bi mechanism in which 4,5-diaminovalerate is the second substrate and 4,5-dioxovalerate is an alternative first substrate
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L-glutamate 1-semialdehyde = 5-aminolevulinate
wild-type enzyme and gabaculine-resistant mutant enzyme use a ping-pong bi-bi mechanism in which 4,5-diaminovalerate is a likely intermediate
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L-glutamate 1-semialdehyde = 5-aminolevulinate
catalytic mechanism via external aldimine and Gem-diamine intermediates, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(S)-4-amino-5-oxopentanoate 4,5-aminomutase
Requires pyridoxal phosphate.
CAS REGISTRY NUMBER
COMMENTARY
68518-07-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-4-Amino-5-oxopentanoate
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one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway
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?
4,5-Diaminovalerate
?
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is a substrate for the pyridoxal 5'-phosphate form of the enzyme
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?
4,5-Dioxovalerate
5-Amino-4-oxopentanoate
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is a substrate for the pyridoxamine form of the enzyme
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?
(S)-4-Amino-5-oxopentanoate
5-Amino-4-oxopentanoate
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anomalous enantiomeric reaction with the (R)enantiomer
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?
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
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involved in conversion of glutamate to 5-aminolevulinate
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-4-amino-5-oxopentanoate
5-aminolevulinate
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involved in conversion of glutamate to 5-aminolevulinate
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r
(S)-4-Amino-5-oxopentanoate
?
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one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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dependent on, during the catalytic cycle, the cofactor undergoes conversion from pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate, conformational changes and binding structures, overview
pyridoxamine 5'-phosphate
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the pyridoxal-phosphate form of the enzyme and the pyridoxamine-phosphate form of the enzyme are similarly active
vitamin B6
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wild-type enzyme and gabaculine-resistant mutant enzyme contain vitamin B6
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
gabaculine
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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 30°C either for several hours with gabaculine alone or for a few min with both gabaculine and glutamate-1-semialdehyde
gabaculine
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wild-type enzyme is inhibited, gabaculine-resistant mutant enzyme is not inhibited
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme and gabaculine-resistant mutant enzyme, overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Henning, M.; Grimm, B.; Jenny, M.; Muller, R.; Jansonius, J.N.
Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus
J. Mol. Biol.
242
591-594
1994
Synechococcus sp.
Rieble, S.; Beale, S.I.
Separation and partial characterization of enzymes catalyzing delta-aminolevulinic acid formation in Synechocystis sp. PCC 6803
Arch. Biochem. Biophys.
289
289-297
1991
Synechococcus sp.
Grimm, B.; Bull, A.; Welinder, K.G.; Gough, S.P.; Kannangara, C.G.
Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and Synechococcus
Carlsberg Res. Commun.
54
67-79
1989
Hordeum vulgare, Synechococcus sp.
Bull, A.D.; Breu, V.; Kannangara, C.G.; Rogers, L.J.; Smith, A.J.
Cyanobacterial glutamate 1-semialdehyde aminotransferase: requirement for pyridoxal phosphate
Arch. Microbiol.
154
56-59
1990
Synechococcus sp.
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Smith, M.A.; Grimm, B.
Gabaculine resistance of Synechococcus glutamate 1-semialdehyde aminotransferase
Biochemistry
31
4122-4127
1992
Synechococcus sp.
Smith, M.A.; Kannangara, C.G.; Grimm, B.
Glutamate 1-semialdehyde aminotransferase: anomalous enantiomeric reaction and enzyme mechanism
Biochemistry
31
11249-11254
1992
Synechococcus sp.
Mayer, S.M.; Rieble, S.; Beale, S.I.
Metal requirement of the enzymes catalyzing conversion of glutamate to delta-aminolevulinic acid in extracts of Chlorella vulgaris and Synechocystis sp. PCC 6803
Arch. Biochem. Biophys.
312
203-209
1994
Chlorella vulgaris, Synechococcus sp.
Brody, S.; Andersen, J.S.; Kannangara, C.G.; Meldgaard, M.; Roepstorff, P.; von Wettstein, D.
Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry
Biochemistry
34
15918-15924
1995
Synechococcus sp.
Smith, M.A.; Kannangara, C.G.; Grimm, B.; von Wettstein, D.
Characterization of glutamate-1-semialdehyde aminotransferase of Synechococcus. Steady-state kinetic analysis
Eur. J. Biochem.
202
749-757
1991
Synechococcus sp.
Grimm, H.M.; Contestabile, R.; John, R.A.; Jansonius, J.N.
Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active reactivity
Proc. Natl. Acad. Sci. USA
84
4866-4871
1997
Synechococcus sp.
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Smith, M.A.; King, P.J.; Grimm, B.
Transient-state kinetic analysis of Synechococcus glutamate 1-semialdehyde aminotransferase
Biochemistry
37
319-329
1998
Synechococcus sp.
Stetefeld, J.; Jenny, M.; Burkhard, P.
Intersubunit signaling in glutamate-1-semialdehyde-aminomutase
Proc. Natl. Acad. Sci. USA
103
13688-13693
2006
Synechococcus sp. (P24630)
Orriss, G.L.; Patel, T.R.; Sorensen, J.; Stetefeld, J.
Absence of a catalytic water confers resistance to the neurotoxin gabaculine
FASEB J.
24
404-414
2010
Synechococcus sp. (P24630)
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