Literature summary for 2.4.2.28 extracted from

Appleby, T.C.; Mathews, I.I.; Porcelli, M.; Cacciapuoti, G.; Ealick, S.E.
Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus (2001), J. Biol. Chem., 276, 39232-39242.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals are grown at either room temperature or 18°C using the hanging drop vapor diffusion technique. Determination of the structure of 5'-deoxy-5'-methylthioadenosine phosphorylase alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP is refined at 2.5 A resolution and the structures of the complexes are refined at resolutions ranging from 1.6 A to 2.0 A	Saccharolobus solfataricus

Crystallization (Comment)

Organism

crystals are grown at either room temperature or 18°C using the hanging drop vapor diffusion technique. Determination of the structure of 5'-deoxy-5'-methylthioadenosine phosphorylase alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP is refined at 2.5 A resolution and the structures of the complexes are refined at resolutions ranging from 1.6 A to 2.0 A

Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	-	-	-
Saccharolobus solfataricus	P50389	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli	Saccharolobus solfataricus

Reaction

Reaction	Comment	Organism	Reaction ID
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate	catalytic mechanism	Saccharolobus solfataricus	a
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate	active and substrate-binding sites, three-dimensional structures	Saccharolobus solfataricus	a
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate	subunit structure, model	Saccharolobus solfataricus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'-deoxy-5'-methylthioadenosine + phosphate	substrate-induced conformational change involving Glu163, which is located at the interface between subunits and swings in toward the active site upon nucleoside binding	Saccharolobus solfataricus	adenine + 5-methylthio-D-ribose 1-phosphate	-	?
5'-deoxy-5'-methylthioadenosine + phosphate	the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates	Saccharolobus solfataricus	adenine + 5-methylthio-D-ribose 1-phosphate	-	?

Subunits

Subunits	Comment	Organism
hexamer	-	Saccharolobus solfataricus
More	enzyme is formed by a trimer of dimers with three symmetric intersubunit disulfide bonds linking the dimers to one another, each monomer contains one active site, which is located near a dimer interface	Saccharolobus solfataricus

Synonyms

Synonyms	Comment	Organism
5'-deoxy-5'-methylthioadenosine phosphorylase	-	Saccharolobus solfataricus
SsMTAP	-	Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
120	-	-	Saccharolobus solfataricus
120	-	recombinant enzyme	Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	disulfide linkages play a key role in thermal stability	Saccharolobus solfataricus
100	-	2 h, stable	Saccharolobus solfataricus
110	-	recombinant enzyme, 2 h, stable	Saccharolobus solfataricus
120	-	-	Saccharolobus solfataricus