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Literature summary for 5.1.1.18 extracted from

  • Zou, L.; Song, Y.; Wang, C.; Sun, J.; Wang, L.; Cheng, B.; Fan, J.
    Crystal structure of maize serine racemase with pyridoxal 5-phosphate (2016), Acta Crystallogr. Sect. F, 72, 165-171 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparisons, cloning from leaf DNA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Zea mays

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, 100 mM NaCl, 10% glycerol, pH 8.0, with 0.001 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, 18% PEG 8000, equilibration agains 0.2 ml of reservoir solution, at 4°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement based on the Rattus norvegicus serine racemase, PDB ID 3hmk Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
82000
-
recombinant His6-tagged enzyme, gel filtration Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine Zea mays
-
D-serine
-
r

Organism

Organism UniProt Comment Textmining
Zea mays F5CAQ9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Zea mays

Reaction

Reaction Comment Organism Reaction ID
L-serine = D-serine reversible racemization and irreversible dehydration reactions are catalyzed by eukaryotic serine racemase, overview Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
-
Zea mays D-serine
-
r

Subunits

Subunits Comment Organism
homodimer 2 * 35000, recombinant His6-tagged enzyme, SDS-PAGE Zea mays

Synonyms

Synonyms Comment Organism
Zm-SR
-
Zea mays
ZmSR
-
Zea mays

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, dependent on, the PLP is bound to each monomer by forming a Schiff base with Lys67 Zea mays

General Information

General Information Comment Organism
evolution the enzyme from Zea mays belongs to the type II PLP-dependent enzymes and differs from the enzyme of a vancomycin-resistant bacterium Zea mays
additional information structural comparison with Rattus norvegicus and Schizosaccharomyces pombe serine racemases reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix, structure modeling, overview. Active site structure comparisons Zea mays
physiological function the enzyme is responsible for D-serine biosynthesis in vivo Zea mays