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1.2.1.31: L-aminoadipate-semialdehyde dehydrogenase

This is an abbreviated version!
For detailed information about L-aminoadipate-semialdehyde dehydrogenase, go to the full flat file.

Word Map on EC 1.2.1.31

Reaction

(S)-2-amino-6-oxohexanoate
+
NAD(P)+
+
H2O
=
L-2-aminoadipate
+
NAD(P)H
+
H+

Synonyms

2-aminoadipate semialdehyde dehydrogenase, 2-aminoadipic 6-semialdehyde dehydrogenase, 2-aminoadipic semialdehyde dehydrogenase, AAR, AASADH, adipic 6-semialdehyde dehydrogenase, aldehyde dehydrogenase 7A1, Aldh7a1, alpha-AAR, alpha-AASA dehydrogenase, alpha-aminoadipate reductase Lys1p, alpha-aminoadipate semialdehyde dehydrogenase, alpha-aminoadipate-semialdehyde dehydrogenase, alpha-aminoadipic acid-delta-semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, Alpha-AR, antiquitin, dehydrogenase, aminoadipate semialdehyde, human U26, L-alpha-aminoadipate delta-semialdehyde oxidoreductase, L-alpha-aminoadipate delta-semialdehyde:NAD oxidoreductase, L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase, L-aminoadipate-semialdehyde dehydrogenase, Lys1p, Nalpha-Z-L-AASA dehydrogenase, U26

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.31 L-aminoadipate-semialdehyde dehydrogenase

Molecular Weight

Molecular Weight on EC 1.2.1.31 - L-aminoadipate-semialdehyde dehydrogenase

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
dimeric enzyme, gel filtration and mass spectrometry
154900
-
analysis of the nucleotide sequence of the 5.1-kb region
155000
160000
-
gel filtration
171000
-
gel filtration
180000
-
gel filtration
184000
tetrameric enzyme, gel filtration and mass spectrometry
222000
tetrameric enzyme, about, sequence calculation
250000
-
gel filtration
31000
-
Lys5 from induced E. coli cells
additional information
wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium. For reference, the dimer Mr is 111 kDa. Wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium