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Information on EC 1.2.1.73 - sulfoacetaldehyde dehydrogenase for references in articles please use BRENDA:EC1.2.1.73Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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sulfoacetaldehyde dehydrogenase
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2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
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sulfoacetaldehyde degradation II
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Taurine and hypotaurine metabolism
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2-sulfoacetaldehyde:NAD+ oxidoreductase
This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
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NAD-coupled sulfoacetaldehyde dehydrogenase
additional information
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the enzyme belongs to the NAD-dependent aldehyde dehydrogenase superfamily
NAD-coupled sulfoacetaldehyde dehydrogenase
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NAD-coupled sulfoacetaldehyde dehydrogenase
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;
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formerly Oceanospirillum sp., CCUG 52065, a marine gammaproteobacterium, strain MED92, gene safD encoding an inducible enzyme
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brenda
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brenda
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brenda
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NAD(P)H + H+
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the enzyme is specific for sulfoacetaldehyde, NAD+ is the highly preferred cofactor to NADP+
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
additional information
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the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
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NAD+ is the highly preferred cofactor
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2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
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NAD+ is the highly preferred cofactor
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
additional information
?
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the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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?
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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?
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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?
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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?
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
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sulfoacetaldehyde is derived from taurine by taurine dehydrogenase, overview
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NAD+
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highly preferred cofactor
NAD+
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highly preferred cofactor
NADP+
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low activity
NADP+
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low activity and inhibition at higher concentration
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Mg2+
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NADP+
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low activity an inhibition at higher concentration
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0.026
2-sulfoacetaldehyde
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pH 9.0, 22°C
0.49
Sulfoacetaldehyde
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pH 9.0, 22°C
0.092
NAD+
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pH 9.0, 22°C
4.5
NADP+
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pH 9.0, 22°C
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9
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7.2 - 10.5
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50% of maximal activity at pH 7.2, 70% at pH 8.0, and 80% at pH 9.5-10.5
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22
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assay at room temperature
22
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assay at room temperature
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growth with taurine (2-aminoethanesulfonate) as the sole source of combined nitrogen under aerobic conditions
brenda
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growth with taurine (2-aminoethanesulfonate) as the sole source of combined nitrogen under aerobic conditions
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brenda
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brenda
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49100
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
50000
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
196500
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sequence calculation
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tetramer
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
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SafD is stable in Tris-HCl buffer, pH 9.0
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native enzyme 610fold to homogeneity by anion exchange and hydrophobic interaction chromatography
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gene safD, DNA and amino acid sequence determination and analysis, genetic organization
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analysis
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the enzyme is useful for determination of sulfoacetaldehyde concentrations
analysis
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the enzyme is useful for determination of sulfoacetaldehyde concentrations
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SAFD_NEPCE
456
49258
Swiss-Prot
A0A0G4JG32_9BURK
484
52812
TrEMBL
A0A0F0KIN5_9MICO
469
50199
TrEMBL
A0A2H5Z155_9BACT
408
44892
TrEMBL
A0A2P9F6S0_9ACTN
481
50937
TrEMBL
A0A2H5WQD8_9BACT
284
30917
TrEMBL
A0A2S6QD75_9PROT
465
50096
TrEMBL
A0A0F0LL37_9MICO
471
49843
TrEMBL
A0A2H5WCS7_9BACT
475
51820
TrEMBL
A0A1B2AE00_9SPHN
481
52381
TrEMBL
A0A1V6JM16_9BACT
473
51458
TrEMBL
A0A2S5CUS7_LYSSH
475
51394
TrEMBL
A0A2M9NG52_9BACL
474
50635
TrEMBL
A0A0B0HEC1_9BACI
186
20652
TrEMBL
A0A1S1HG31_9SPHN
478
51659
TrEMBL
A0A2K8R237_9ACTN
486
51682
TrEMBL
A0A1Y5TTC9_9RHOB
127
14032
TrEMBL
A0A1Y2MTW7_STRPT
486
51304
TrEMBL
A0A0D1D8L3_9RHOB
460
47284
TrEMBL
A0A100JAK1_9ACTN
481
50478
TrEMBL
A0A1Y2MHR3_PSEAH
480
49847
TrEMBL
A0A0F0KG09_9MICO
469
49723
TrEMBL
A0A166DWK4_9EURY
474
51766
TrEMBL
A0A161GH56_RHOFA
482
51232
TrEMBL
A0A0P1IQL9_9RHOB
462
49455
TrEMBL
A0A2K8QXF7_9ACTN
497
52719
TrEMBL
A0A1U9Z485_9RHIZ
492
53396
TrEMBL
A0A2H5VUK3_9BACT
275
30094
TrEMBL
A0A1Q2Z8V5_9ACTN
466
49361
TrEMBL
A0A0M2HD54_9MICO
470
50416
TrEMBL
A0A1V5WZB2_9DELT
476
52532
TrEMBL
A0A2U3N0E4_9GAMM
483
53110
TrEMBL
A0A290H9V1_9PROT
472
51512
TrEMBL
A0A0F0LL07_9MICO
469
50083
TrEMBL
A0A2S6RW91_9PROT
470
50372
TrEMBL
A0A0N0Z5B5_9BACI
475
51303
TrEMBL
A0A1V5G716_9BACT
340
37014
TrEMBL
A0A0D8HK14_9ACTN
490
51917
TrEMBL
A0A2H5X2A0_9BACT
474
50696
TrEMBL
A0A2S6SCF4_9PROT
459
51072
TrEMBL
A0A1X9MCP1_9BACI
477
51161
TrEMBL
A0A165T2I1_9RHOB
462
49407
TrEMBL
A0A2H5Y6A3_9BACT
497
54570
TrEMBL
A0A2N7QUH0_9GAMM
476
52277
TrEMBL
A0A2H5YSG5_9BACT
479
53094
TrEMBL
A0A100JI77_STRSC
476
50074
TrEMBL
A4A508_9GAMM
455
49271
TrEMBL
A0A021WY44_9RHIZ
466
48530
TrEMBL
A0A2H5YEM2_9BACT
203
22158
TrEMBL
A0A166EQC5_9RHOB
461
49963
TrEMBL
A0A1A8TU21_9GAMM
476
51649
TrEMBL
A0A1Y2MNR1_PSEAH
485
51537
TrEMBL
A0A2S6SNF3_9PROT
479
52737
TrEMBL
A0A1V5FL41_9BACT
245
27083
TrEMBL
A0A221UW53_9FLAO
475
52139
TrEMBL
A0A0P1H6W8_9RHOB
461
49182
TrEMBL
A0A1C9W9X1_9GAMM
477
51874
TrEMBL
A0A1R3TU56_9RHIZ
469
50344
TrEMBL
A0A1Y5TZN9_9RHOB
461
49373
TrEMBL
A0A1S9CZB0_9GAMM
271
29409
TrEMBL
A0A2U3MK73_9NEIS
501
55244
TrEMBL
A0A1Y5T908_9PROT
484
51390
TrEMBL
A0A165UE53_9RHOB
461
49722
TrEMBL
A0A1C9W8M7_9GAMM
455
49151
TrEMBL
A0A1U9Z914_9RHIZ
466
48551
TrEMBL
A0A0F0L9Y9_9MICO
500
53338
TrEMBL
A0A0P0MFM7_9BURK
485
53528
TrEMBL
A0A2P8AZG7_9ACTN
479
50104
TrEMBL
A0A1V5PKR1_9BACT
473
51793
TrEMBL
A0A178X9R4_9PSEU
474
49601
TrEMBL
A0A1Y2P440_STRFR
481
50868
TrEMBL
A0A2H5VXF4_9BACT
474
51933
TrEMBL
A0A1H8WI64_9RHIZ
469
50519
TrEMBL
A0A1Y2MT98_PSEAH
483
50641
TrEMBL
A0A150HJE3_9GAMM
480
52428
TrEMBL
A0A2H5ZSD9_9BACT
165
18350
TrEMBL
A0A2H6FZG6_9BACT
478
51385
TrEMBL
A0A223Z1D4_9EURY
470
50658
TrEMBL
A0A0U5B2G3_9BACL
481
52220
TrEMBL
A0A2S6QE40_9PROT
480
51723
TrEMBL
A0A2H5Z3F8_9BACT
478
53008
TrEMBL
A0A2K8PDE4_STRLA
481
50982
TrEMBL
A0A2H5VIU2_9BACT
474
51918
TrEMBL
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Weinitschke, S.; von Rekowski, K.S.; Denger, K.; Cook, A.M.
Sulfoacetaldehyde is excreted quantitatively by Acinetobacter calcoaceticus SW1 during growth with taurine as sole source of nitrogen
Microbiology
151
1285-1290
2005
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Denger, K.; Weinitschke, S.; Hollemeyer, K.; Cook, A.M.
Sulfoacetate generated by Rhodopseudomonas palustris from taurine
Arch. Microbiol.
182
254-258
2004
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Krejcik, Z.; Denger, K.; Weinitschke, S.; Hollemeyer, K.; Paces, V.; Cook, A.M.; Smits, T.H.
Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase
Arch. Microbiol.
190
159-168
2008
Neptuniibacter caesariensis
brenda
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