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Literature summary for 2.8.2.37 extracted from

  • Mougous, J.D.; Petzold, C.J.; Senaratne, R.H.; Lee, D.H.; Akey, D.L.; Lin, F.L.; Munchel, S.E.; Pratt, M.R.; Riley, L.W.; Leary, J.A.; Berger, J.M.; Bertozzi, C.R.
    Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis (2004), Nat. Struct. Mol. Biol., 11, 721-729.
    View publication on PubMed
Search for more literature for 2.8.2.37

Cloned(Commentary)

Cloned (Comment) Organism
Stf0 gene is amplified from Mycobacterium tuberculosis H37Rv and expressed in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method, crystal structure of the enzyme bound to trehalose Mycolicibacterium smegmatis

Protein Variants

Protein Variants Comment Organism
E33A kcat/Km for trehalose is 4.2fold lower compared to wild-type value Mycolicibacterium smegmatis
E36A kcat/Km for trehalose is 34.2fold lower compared to wild-type value Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
18
-
 alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis
29
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose Mycobacterium tuberculosis sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose Mycolicibacterium smegmatis sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis O53699
-
-
Mycolicibacterium smegmatis P84151
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
-
 Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
-
 Mycolicibacterium smegmatis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?
3'-phosphoadenylyl sulfate + alpha,alpha-trehalose sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 Mycolicibacterium smegmatis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
 ?
3'-phosphoadenylyl sulfate + alpha-D-galactopyranosyl alpha-D-glucopyranoside alpha-D-galactopyranosyl-alpha-D-glucopyranoside is a synthetic analog of trehalose epimerized at a single stereocenter is sulfated 68fold less efficiently than trehalose Mycolicibacterium smegmatis ?
-
 ?
additional information no activity on beta-phenyl glucoside, glucose, neo-trehalose or iso-trehalose Mycolicibacterium smegmatis ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.017
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
0.61
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis
1.6
-
 alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis

General Information

General Information Comment Organism
malfunction Mycobacterium tuberculosis deficient in Stf0 lacks both sulfolipid SL-1 and partially modified analogs Mycobacterium tuberculosis
physiological function sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 Mycobacterium tuberculosis
physiological function sulfotransferase Stf0 carries out the first committed step in the biosynthesis of sulfolipid SL-1 Mycolicibacterium smegmatis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0026
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
0.021
-
 alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis
0.89
-
 alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis