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
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5-aminolevulinic
- tetrapyrrole
- glutamyl-trna
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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
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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General Information
General Information on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase
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evolution
physiological function
additional information
evolution
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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the enzyme is a member of the GSAM family
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co-expression of hemL with hemAM achieves asignificantly increased 5-aminolevulinate production
physiological function
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co-expression of hemL with hemAM achieves asignificantly increased 5-aminolevulinate production
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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
additional information
structure-function analysis., overview. Enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation. The mobility of residues Gly163, Ser164 and Gly165 is important for reorientation of the gating loop. The asymmetry of the AtGSA1 structure supports the previously proposed negative cooperativity between monomers of GSAM
additional information
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structure-function analysis., overview. Enzyme AtGSA1 forms an asymmetric dimer and displays asymmetry in cofactor binding as well as in the gating-loop orientation. The mobility of residues Gly163, Ser164 and Gly165 is important for reorientation of the gating loop. The asymmetry of the AtGSA1 structure supports the previously proposed negative cooperativity between monomers of GSAM
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, overview. 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
additional information
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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three-dimensional structure analysis of wild-type and mutant enzymes, overview. 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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