Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Goncalves, S.; Esteves, A.M.; Santos, H.; Borges, N.; Matias, P.M.
    The three-dimensional structure of mannosyl-3-phosphoglycerate phosphatase from Thermus thermophilus HB27: a new member of the haloalkanoic acid dehalogenase superfamily (2011), Biochemistry, 50, 9551-9567.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.70 expression in Escherichia coli strain BL21 (DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.70 purified recombinant enzyme in apo-form and in complex with substrates, substrate analogues and inhibitors, sitting drop vapor diffusion technique, 10 mg/ml protein in 20 mM MES-NaOH pH 6.3, 760 mM NaCl, 5 mM DTT, 1 mM EDTA, 5 mM Mg2+ and Na/KPO4, is mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis, molecular replacement Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.70 Mg2+ dependent on Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.70 Thermus thermophilus Q72K29
-
-
3.1.3.70 Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 Q72K29
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.70 recombinant enzyme from Escherichia coli strain BL21 (DE3) by cation exchange chromatography Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.70 2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate in Thermus thermophilus strain HB27 MpgP the phosphoryl-transfer undergoes a concerted DNSN mechanism with assistance of proton transfer from the general acid Asp8, forming a short-lived PO3- intermediate which is attacked by a nucleophilic water molecule, structure-activity relationship analysis, overview Thermus thermophilus
a

Subunits

EC Number Subunits Comment Organism
3.1.3.70 More detailed structure analysis, overview Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.1.3.70 More the enzyme is a member of the haloalkanoic acid dehalogenase superfamily. It is a metal-dependent haloalcanoic acid dehalogenase-like phosphatase, preserving the catalytic Motifs I-IV of the HAD-core domain, and classified as a Cof-type MPGP based on its C2B cap insertion module Thermus thermophilus
3.1.3.70 MPGP
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
3.1.3.70 metabolism mannosyl-3-phosphoglycerate phosphatase is the enzyme involved in the second step of the two-step mannosyl-3-phosphoglycerate biosynthetic pathway, most commonly found in (hyper)thermophilic microorganisms Thermus thermophilus
3.1.3.70 additional information two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket Thermus thermophilus
3.1.3.70 physiological function mannosyl-3-phosphoglycerate phosphatase is a key mediator in the physiological response to thermal and osmotic stresses, catalyzing the hydrolysis of mannosyl-3-phosphoglycerate into the final product, alpha-mannosylglycerate Thermus thermophilus