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Information on EC 1.1.1.373 - sulfolactaldehyde 3-reductase
for references in articles please use BRENDA:EC1.1.1.373
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.373 sulfolactaldehyde 3-reductase
IUBMB Comments
The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
showSynonyms
3-sulfolactaldehyde reductase, 3-sulpholactaldehyde reductase, NADH-dependent SLA reductase, SLA reductase, sulfolactaldehyde reductase, yihU, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-sulpholactaldehyde reductase
SLA reductase
yihU
yihU
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-dihydroxypropane-1-sulfonate + NAD+ = 2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
-
-
-
-
2,3-dihydroxypropane-1-sulfonate + NAD+ = 2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
rapid equilibrium sequential Bi-Bi mechanism, dynamic domain movements occurs during catalysis. A conserved sulfonate pocket in SLA reductase recognizes the sulfonate oxygens through hydrogen bonding to Asn174, Ser178, and the backbone amide of Arg123, along with an ordered water molecule
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SYSTEMATIC NAME
IUBMB Comments
2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase
The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-sulfolactaldehyde + NADH + H+
(S)-2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
?
2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
3-sulfolactaldehyde + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
3-sulfolactaldehyde + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: NADP+ is not a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the SLA reductase shows no detectable activity on the analogous glycolytic intermediate glyceraldehyde-3-phosphate. Substrate binding analysis
Products: -
Products: -
-
additional information
?
-
Substrates: NADP+ is not a substrate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-sulfolactaldehyde + NADH + H+
(S)-2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
?
2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
3-sulfolactaldehyde + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
3-sulfolactaldehyde + NADH + H+
2,3-dihydroxypropane-1-sulfonate + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: NADP+ is not a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: NADP+ is not a substrate
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
modified NADH analogues are inhibitors of YihU
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics analysis and kinetic mechanism, overview
-
1.63
(S)-3-sulfolactaldehyde
mutant enzyme G122S, at pH 8.0 and 30°C
-
5.74
(S)-3-sulfolactaldehyde
mutant enzyme T124G, at pH 8.0 and 30°C
-
7.99
(S)-3-sulfolactaldehyde
mutant enzyme R123G, at pH 8.0 and 30°C
-
0.3
2-hydroxy-3-oxopropane-1-sulfonate
wild-type enzyme, pH and temperature not specified in the publication
1.63
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant G122S, pH and temperature not specified in the publication
5.74
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant T124G, pH and temperature not specified in the publication
7.99
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant R123G, pH and temperature not specified in the publication
0.009
NADH
enzyme mutant R123G, pH and temperature not specified in the publication
0.023
NADH
enzyme mutant T124G, pH and temperature not specified in the publication
0.082
NADH
wild-type enzyme, pH and temperature not specified in the publication
0.123
NADH
enzyme mutant G122S, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant T124G, pH and temperature not specified in the publication
68
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant R123G, pH and temperature not specified in the publication
71
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant G122S, pH and temperature not specified in the publication
332
2-hydroxy-3-oxopropane-1-sulfonate
wild-type enzyme, pH and temperature not specified in the publication
12.7
NADH
enzyme mutant T124G, pH and temperature not specified in the publication
22.1
NADH
enzyme mutant R123G, pH and temperature not specified in the publication
178
NADH
enzyme mutant G122S, pH and temperature not specified in the publication
548
NADH
wild-type enzyme, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
(S)-3-sulfolactaldehyde
mutant enzyme T124G, at pH 8.0 and 30°C
-
8.5
(S)-3-sulfolactaldehyde
mutant enzyme R123G, at pH 8.0 and 30°C
-
4.7
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant T124G, pH and temperature not specified in the publication
8.5
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant R123G, pH and temperature not specified in the publication
43.6
2-hydroxy-3-oxopropane-1-sulfonate
enzyme mutant G122S, pH and temperature not specified in the publication
1106.7
2-hydroxy-3-oxopropane-1-sulfonate
wild-type enzyme, pH and temperature not specified in the publication
552.2
NADH
enzyme mutant T124G, pH and temperature not specified in the publication
1447.2
NADH
enzyme mutant G122S, pH and temperature not specified in the publication
2455.6
NADH
enzyme mutant R123G, pH and temperature not specified in the publication
6682.9
NADH
wild-type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.63
hexahydronicotinamide adenine dinucleotide
wild type enzyme, at pH 8.0 and 30°C
-
1.81
tetrahydronicotinamide adenine dinucleotide
wild type enzyme, at pH 8.0 and 30°C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.3
hexahydro-NADH
Escherichia coli
wild-type enzyme, pH and temperature not specified in the publication
-
10.3
hexahydronicotinamide adenine dinucleotide
Escherichia coli
wild type enzyme, at pH 8.0 and 30°C
-
4.03
tetrahydro-NADH
Escherichia coli
wild-type enzyme, pH and temperature not specified in the publication
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
based on conserved sequence motifs, enzyme SLA reductase is assigned to the beta-hydroxyacid dehydrogenase (beta-HAD) family, comparisons of typical sequence motifs. SLA reductases form a separate subgroup with conserved sulfonate substrate-binding sequence at residues 122-124 (YihU numbering). SLA reductases share beta-HAD sequence motifs but possess a unique sulfonate substrate-binding sequence (extended motif-2 [D/EVPVGRTXX-XAXXG])
physiological function
2,3-dihydroxypropanesulfonate (DHPS) is a major sulfur species in the biosphere. One important route for the production of DHPS is sulfoglycolytic catabolism of sulfoquinovose (SQ) through the Embden-Meyerhof-Parnas (sulfo-EMP) pathway. SQ is a sulfonated carbohydrate present in plant and cyanobacterial sulfolipids (sulfoquinovosyl diacylglyceride and its metabolites) and is biosynthesized globally at a rate of around 10 billion tons per annum. The final step in the bacterial sulfo-EMP pathway involves reduction of sulfolactaldehyde (SLA) to DHPS, catalyzed by the NADH-dependent SLA reductase
additional information
a conserved sulfonate pocket in SLA reductase recognizes the sulfonate oxygens through hydrogen bonding to Asn174, Ser178, and the backbone amide of Arg123, along with an ordered water molecule. This triad of residues distinguishes these enzymes from classical beta-HADs that act on carboxylate substrates. Determination of the structural basis for cofactor binding and sulfonate recognition, dynamic structural changes occur during catalysis
Show AA Sequence and Transmembrane Helices (994 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
YihU forms a dimer of intimate homodimer pairs. The enzyme exuísts as a tetramer in crystal and in solution. Within the asymmetric unit, each protomer adopts a two-domain architecture containing an N-terminal nucleotide-binding domain (residues 1-164) and a C-terminal helical bundle (residues 165-294) both connected by the long interdomain helix alpha8. The N-terminal domain is composed of a classical alpha/beta Rossmann fold (composed of an extended sheet formed by beta1-6, flanked by alpha1-5 in a three-layered sandwich) appended with an additional beta-alpha-beta motif containing beta7-9 and alpha6. Four interfaces are present within the subunits of the YihU tetramer. Detailed structure analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme, hanging drop vapor diffusion method, using 25% (w/v) PEG (polyethylene glycol) 1500, 0.1 M sodium malonate dibasic monohydrate, imidazole, boric acid buffer pH 4.0. NADH-bound enzyme, hanging drop vapor diffusion method, using 25% (w/v) PEG (polyethylene glycol) 3350, 0.2 M CH3COONH4, 0.1 M Bis-Tris pH 6.5. NADH- and (S)-2,3-dihydroxypropane-1-sulfonate-bound enzyme, hanging drop vapor diffusion method, using 32% (w/v) PEG 3350, 0.2 mM CH3COONH4, 0.1 M Bis-Tris pH 6.5
purified enzyme in its apo and cofactor-bound states, as well as in ternary complex YihU-NADH-DHPS with the cofactor and product bound in the active site, X-ray diffraction structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G122S
R123G
T124G
G122S
the mutant shows reduced activity compared to the wild type enzyme
G122S
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
R123G
the mutant shows reduced activity compared to the wild type enzyme
R123G
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
T124G
the mutant shows reduced activity compared to the wild type enzyme
T124G
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Denger, K.; Weiss, M.; Felux, A.; Schneider, A.; Mayer, C.; Spiteller, D.; Huhn, T.; Cook, A.; Schleheck, D.
Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle
Nature
507
114-117
2014
Escherichia coli (P0A9V8), Escherichia coli MG1655 (P0A9V8)
brenda
Sharma, M.; Abayakoon, P.; Lingford, J.; Epa, R.; John, A.; Jin, Y.; Goddard-Borger, E.; Davies, G.; Williams, S.
Dynamic structural changes accompany the production of dihydroxypropanesulfonate by sulfolactaldehyde reductase
ACS Catal.
10
2826-2836
2020
Escherichia coli (P0A9V8)
-
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.373)
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Release 2023.1 (January 2023)
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