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
-
five-carbon
-
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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Reaction
Reaction on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase
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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
intermolecular transamination occurs during conversion of (S)-4-amino-5-oxopentanoate to 5-amino-4-oxopentanoate
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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
the catalytic mechanism includes enzyme-bound diaminovalerate as a central intermediate
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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
catalytic mechanism via external aldimine and Gem-diamine intermediates, overview
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