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Literature summary for 1.1.1.373 extracted from

  • 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 (2020), ACS Catal., 10, 2826-2836 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli
gene yihU, phylogenetic analysis and tree Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli
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 Escherichia coli

Protein Variants

Protein Variants Comment Organism
G122S the mutant shows reduced activity compared to the wild type enzyme Escherichia coli
G122S site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Escherichia coli
R123G the mutant shows reduced activity compared to the wild type enzyme Escherichia coli
R123G site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Escherichia coli
T124G the mutant shows reduced activity compared to the wild type enzyme Escherichia coli
T124G site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
hexahydro-NADH
-
Escherichia coli
hexahydronicotinamide adenine dinucleotide
-
Escherichia coli
additional information modified NADH analogues are inhibitors of YihU Escherichia coli
tetrahydro-NADH
-
Escherichia coli
tetrahydronicotinamide adenine dinucleotide
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics analysis and kinetic mechanism, overview Escherichia coli
0.009
-
NADH enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
0.009
-
NADH mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli
0.023
-
NADH enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
0.023
-
NADH mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
0.082
-
NADH wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli
0.082
-
NADH wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
0.123
-
NADH enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
0.123
-
NADH mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
0.3
-
(S)-3-sulfolactaldehyde wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli
0.3
-
2-hydroxy-3-oxopropane-1-sulfonate wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
1.63
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
1.63
-
(S)-3-sulfolactaldehyde mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
5.74
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
5.74
-
(S)-3-sulfolactaldehyde mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
7.99
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
7.99
-
(S)-3-sulfolactaldehyde mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
123000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-3-sulfolactaldehyde + NADH + H+ Escherichia coli
-
(S)-2,3-dihydroxypropane-1-sulfonate + NAD+
-
?
2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+ Escherichia coli
-
2,3-dihydroxypropane-1-sulfonate + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9V8
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex 75 gel filtration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
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 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-sulfolactaldehyde + NADH + H+
-
Escherichia coli (S)-2,3-dihydroxypropane-1-sulfonate + NAD+
-
?
2-hydroxy-3-oxopropane-1-sulfonate + NADH + H+
-
Escherichia coli 2,3-dihydroxypropane-1-sulfonate + NAD+
-
r
additional information the SLA reductase shows no detectable activity on the analogous glycolytic intermediate glyceraldehyde-3-phosphate. Substrate binding analysis Escherichia coli ?
-
-

Subunits

Subunits Comment Organism
homotetramer 4 * 30000, calculated from amino acid sequence Escherichia coli
tetramer YihU forms a dimer of intimate homodimer pairs. The enzyme exu├şsts 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 Escherichia coli

Synonyms

Synonyms Comment Organism
3-sulfolactaldehyde reductase UniProt Escherichia coli
NADH-dependent SLA reductase
-
Escherichia coli
SLA reductase
-
Escherichia coli
sulfolactaldehyde reductase
-
Escherichia coli
yihU
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
12.7
-
NADH enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
12.7
-
NADH mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
22.1
-
NADH enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
22.1
-
NADH mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli
27
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
27
-
(S)-3-sulfolactaldehyde mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
68
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
68
-
(S)-3-sulfolactaldehyde mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli
71
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
71
-
(S)-3-sulfolactaldehyde mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
178
-
NADH enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
178
-
NADH mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
332
-
2-hydroxy-3-oxopropane-1-sulfonate wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
332
-
(S)-3-sulfolactaldehyde wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli
548
-
NADH wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
548
-
NADH wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information cofactor binding analysis Escherichia coli
NAD+
-
Escherichia coli
NADH
-
Escherichia coli
NADH dependent on Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.81
-
tetrahydronicotinamide adenine dinucleotide wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli
4.63
-
hexahydronicotinamide adenine dinucleotide wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.03
-
wild-type enzyme, pH and temperature not specified in the publication Escherichia coli tetrahydro-NADH
4.03
-
wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli tetrahydronicotinamide adenine dinucleotide
10.3
-
wild-type enzyme, pH and temperature not specified in the publication Escherichia coli hexahydro-NADH
10.3
-
wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli hexahydronicotinamide adenine dinucleotide

General Information

General Information Comment Organism
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]) Escherichia coli
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 Escherichia coli
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 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.7
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
4.7
-
(S)-3-sulfolactaldehyde mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
8.5
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
8.5
-
(S)-3-sulfolactaldehyde mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli
43
-
(S)-3-sulfolactaldehyde mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
43.6
-
2-hydroxy-3-oxopropane-1-sulfonate enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
552.2
-
NADH enzyme mutant T124G, pH and temperature not specified in the publication Escherichia coli
570
-
NADH mutant enzyme T124G, at pH 8.0 and 30┬░C Escherichia coli
1090
-
(S)-3-sulfolactaldehyde wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli
1106.7
-
2-hydroxy-3-oxopropane-1-sulfonate wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
1447.2
-
NADH enzyme mutant G122S, pH and temperature not specified in the publication Escherichia coli
1450
-
NADH mutant enzyme G122S, at pH 8.0 and 30┬░C Escherichia coli
2360
-
NADH mutant enzyme R123G, at pH 8.0 and 30┬░C Escherichia coli
2455.6
-
NADH enzyme mutant R123G, pH and temperature not specified in the publication Escherichia coli
6682.9
-
NADH wild-type enzyme, pH and temperature not specified in the publication Escherichia coli
6720
-
NADH wild type enzyme, at pH 8.0 and 30┬░C Escherichia coli