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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.2.37 6.4
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
2.8.2.37 18
-
alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis
2.8.2.37 29
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.2.37 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
-
?
2.8.2.37 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

EC Number Organism UniProt Comment Textmining
2.8.2.37 Mycobacterium tuberculosis O53699
-
-
2.8.2.37 Mycolicibacterium smegmatis P84151
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.2.37
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.37 3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
-
Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
?
2.8.2.37 3'-phosphoadenylyl sulfate + alpha,alpha-trehalose
-
Mycolicibacterium smegmatis adenosine 3',5'-bisphosphate + 2-O-sulfo-alpha,alpha-trehalose
-
?
2.8.2.37 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
-
?
2.8.2.37 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
-
?
2.8.2.37 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 ?
-
?
2.8.2.37 additional information no activity on beta-phenyl glucoside, glucose, neo-trehalose or iso-trehalose Mycolicibacterium smegmatis ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.2.37 0.017
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
2.8.2.37 0.61
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis
2.8.2.37 1.6
-
alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis

General Information

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8.2.37 0.0026
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E36Q Mycolicibacterium smegmatis
2.8.2.37 0.021
-
alpha,alpha-trehalose pH 7.5, 22°C, mutant enzyme E33A Mycolicibacterium smegmatis
2.8.2.37 0.89
-
alpha,alpha-trehalose pH 7.5, 22°C, wild-type enzyme Mycolicibacterium smegmatis