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Muramoylpentapeptide carboxypeptidase

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Muramoylpentapeptide carboxypeptidase
Identifiers
EC no.3.4.17.8
CAS no.9077-67-2
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BRENDABRENDA entry
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MetaCycmetabolic pathway
PRIAMprofile
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NCBIproteins

Muramoylpentapeptide carboxypeptidase (EC 3.4.17.8, D-alanine carboxypeptidase I, DD-carboxypeptidase, D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanine-D-alanine-carboxypeptidase, carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase, D-alanyl-D-alanine peptidase, DD-peptidase, penicillin binding protein 5, PBP5, PdcA, VanY) is an enzyme. This enzyme catalyses the following chemical reaction.

Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl--D-alanine

This bacterial enzyme that requires a divalent cation for activity.

References

  1. Izaki K, Strominger JL (June 1968). "Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". The Journal of Biological Chemistry. 243 (11): 3193–201. PMID 4871206.

External links

Hydrolase: proteases (EC 3.4)
3.4.11-19: Exopeptidase
3.4.11
3.4.13
3.4.14
3.4.15
3.4.16
3.4.17
Metalloexopeptidases
Carboxypeptidase
A
A2
B
C
E
Glutamate II
Other/ungrouped
3.4.21-25: Endopeptidase
3.4.99: Unknown
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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