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
-
aldimine
- glutr
-
five-carbon
-
glutamyl-trnaglu
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trna-dependent
-
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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Cofactor
Cofactor on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase
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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
pyridoxal 5'-phosphate
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure with a Schiff base linkage between the cofactor and the epsilon-amino group of Lys286, overview
pyridoxal 5'-phosphate
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview
pyridoxamine 5'-phosphate
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conversion into the active pyridoxamine-phosphate form of enzyme in an exponential process
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
pyridoxamine 5'-phosphate
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview
pyridoxamine 5'-phosphate
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview
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wild-type enzyme and gabaculine-resistant mutant enzyme contain vitamin B6
during the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation
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additional information
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during the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation
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additional information
in both the pyridoxamine 5'-phosphate- and pyridoxal 5'-phosphate-bound structures, the gating loops are well-defined in electron density and are in the ordered open conformation. The conformation of the gating loop is symmetrical
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