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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.1.18 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.18 82000
-
 recombinant His6-tagged enzyme, gel filtration Zea mays

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.18 Zea mays F5CAQ9
-
-

Purification (Commentary)

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

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.1.1.18 leaf
-
 Zea mays
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
5.1.1.18 Zm-SR
-
 Zea mays
5.1.1.18 ZmSR
-
 Zea mays

Cofactor

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

General Information

EC Number General Information Comment Organism
5.1.1.18 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
5.1.1.18 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
5.1.1.18 physiological function the enzyme is responsible for D-serine biosynthesis in vivo Zea mays