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3.4.17.13: Muramoyltetrapeptide carboxypeptidase

This is an abbreviated version!
For detailed information about Muramoyltetrapeptide carboxypeptidase, go to the full flat file.

Word Map on EC 3.4.17.13

Reaction

hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-/-D-alanine =

Synonyms

Carboxypeptidase II, Carboxypeptidase IIW, Carboxypeptidase, lysyl-D-alanine, Carboxypeptidase, muramoyltetrapeptide, cjj81176_0915, DacB, L,D-carboxypeptidase A, L-Lysyl-D-alanine carboxypeptidase, LD-Carboxypeptidase, LdcA, LdcA1, LdcA2, LdcB, muramoyltetrapeptide carboxypeptidase, peptidase U61, Pgp2, Spr0554

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.13 Muramoyltetrapeptide carboxypeptidase

Crystallization

Crystallization on EC 3.4.17.13 - Muramoyltetrapeptide carboxypeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion using the hanging-drop method. The protein crystallizes in space group I222 and P32(1)2
-
to 1.89 A resolution, abd modeling of interaction with substrate
purified recombinant wild-type enzyme and mutants S115A and H285A, sitting drop vapour diffusion method, 0.004 ml of 6 mg/ml protein containing solution is mixed with an equal volume of reservoir solution containing 20 mM CaCl2 dihydrate, 0.1 M sodium acetate trihydrate, pH 4.6, and 30% v/v 2-methyl-2,4-pentanediol, room temperature, 6 mg/ml selenomethionine-labeled enzyme from 50 mM citric acid, pH 4.5, 21°C, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution