Beta-Ala-Xaa dipeptidase
Details
- Name
- Beta-Ala-Xaa dipeptidase
- Synonyms
- 3.4.13.-
- Beta-Ala-His dipeptidase
- Peptidase V
- Gene Name
- pepV
- Organism
- Lactobacillus delbrueckii subsp. lactis
- Amino acid sequence
>lcl|BSEQ0011139|Beta-Ala-Xaa dipeptidase MDLNFKELAEAKKDAILKDLEELIAIDSSEDLENATEEYPVGKGPVDAMTKFLSFAKRDG FDTENFANYAGRVNFGAGDKRLGIIGHMDVVPAGEGWTRDPFKMEIDEEGRIYGRGSADD KGPSLTAYYGMLLLKEAGFKPKKKIDFVLGTNEETNWVGIDYYLKHEPTPDIVFSPDAEY PIINGEQGIFTLEFSFKNDDTKGDYVLDKFKAGIATNVTPQVTRATISGPDLEAVKLAYE SFLADKELDGSFEINDESADIVLIGQGAHASAPQVGKNSATFLALFLDQYAFAGRDKNFL HFLAEVEHEDFYGKKLGIFHHDDLMGDLASSPSMFDYEHAGKASLLNNVRYPQGTDPDTM IKQVLDKFSGILDVTYNGFEEPHYVPGSDPMVQTLLKVYEKQTGKPGHEVVIGGGTYGRL FERGVAFGAQPENGPMVMHAANEFMMLDDLILSIAIYAEAIYELTKDEEL
- Number of residues
- 470
- Molecular Weight
- 51989.945
- Theoretical pI
- 4.31
- GO Classification
- Functionsdipeptidase activity / metallopeptidase activity / zinc ion bindingComponentscytoplasm
- General Function
- Zinc ion binding
- Specific Function
- Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.
- Pfam Domain Function
- Peptidase_M20 (PF01546)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0003186|1413 bp ATGGACTTAAACTTTAAAGAACTGGCGGAAGCCAAGAAGGACGCGATCTTAAAAGACTTA GAGGAATTGATCGCCATTGACTCTTCAGAAGACCTGGAAAACGCCACGGAAGAATACCCA GTTGGCAAGGGTCCGGTTGACGCCATGACCAAGTTCCTCAGCTTTGCCAAGCGGGACGGC TTTGACACGGAAAACTTCGCCAACTACGCCGGCCGGGTCAACTTCGGTGCAGGCGACAAG CGCCTGGGCATCATCGGCCACATGGACGTAGTGCCAGCTGGTGAAGGCTGGACCCGGGAC CCCTTCAAGATGGAAATCGACGAAGAAGGCCGGATCTACGGCCGGGGCAGCGCCGACGAC AAGGGGCCAAGCTTAACTGCCTACTACGGGATGCTTTTGCTCAAAGAAGCTGGCTTTAAG CCAAAGAAGAAGATCGACTTCGTCTTAGGGACCAACGAAGAAACCAACTGGGTCGGGATC GACTACTACTTGAAGCACGAACCGACTCCAGACATCGTCTTCTCACCAGACGCTGAATAC CCGATCATCAATGGTGAACAAGGGATCTTCACCCTGGAATTCAGCTTCAAGAACGATGAT ACTAAGGGCGACTATGTTTTAGACAAGTTCAAGGCCGGGATTGCCACTAACGTGACTCCG CAGGTTACCCGGGCTACTATCTCTGGACCTGACCTGGAAGCTGTTAAATTGGCTTACGAA AGCTTTTTGGCAGACAAGGAATTGGACGGATCATTTGAAATTAATGACGAAAGCGCCGAT ATCGTCTTGATCGGCCAAGGGGCCCACGCTTCAGCTCCGCAAGTCGGCAAGAACTCAGCA ACCTTCCTGGCCCTCTTCCTGGACCAATACGCTTTTGCCGGCCGGGACAAGAACTTCCTC CACTTCCTGGCTGAAGTGGAACACGAAGACTTCTATGGCAAGAAGCTGGGCATCTTCCAC CACGATGATCTGATGGGCGATCTGGCCAGCAGCCCGTCCATGTTCGACTACGAACACGCC GGCAAGGCCAGCCTCTTGAACAATGTCCGCTACCCGCAAGGGACTGACCCGGACACCATG ATCAAGCAGGTTCTGGACAAGTTCAGCGGCATCCTGGATGTCACTTACAACGGCTTTGAA GAACCGCACTACGTGCCAGGCAGCGACCCAATGGTGCAGACTTTGCTCAAGGTTTACGAA AAACAAACCGGCAAGCCGGGCCACGAAGTCGTAATCGGCGGCGGGACTTACGGCCGCCTC TTTGAGCGCGGGGTTGCCTTCGGGGCCCAGCCGGAAAACGGCCCAATGGTTATGCACGCC GCCAACGAATTCATGATGCTGGACGATTTGATCCTGTCCATCGCTATCTACGCTGAAGCC ATCTACGAATTGACCAAGGACGAAGAGCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P45494 UniProtKB Entry Name PEPV_LACDL GenBank Protein ID 577569 GenBank Gene ID Z31377 - General References
- Vongerichten KF, Klein JR, Matern H, Plapp R: Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme. Microbiology. 1994 Oct;140 ( Pt 10):2591-600. [Article]
- Jozic D, Bourenkow G, Bartunik H, Scholze H, Dive V, Henrich B, Huber R, Bode W, Maskos K: Crystal structure of the dinuclear zinc aminopeptidase PepV from Lactobacillus delbrueckii unravels its preference for dipeptides. Structure. 2002 Aug;10(8):1097-106. [Article]