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Sequence of PRLA_LYSEN

EC Number:3.4.21.12

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
alpha-lytic endopeptidase
P00778
Lysobacter enzymogenes
397
41077
Reaction
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins
Other sequences found for EC No. 3.4.21.12

General information:

Sequence
show sequence in fasta format
  0 MYVSNHRSRR VARVSVSCLV AALAAMSCGA ALAADQVDPQ LKFAMQRDLG IFPTQLPQYL
 60 QTEKLARTQA AAIEREFGAQ FAGSWIERNE DGSFKLVAAT SGARKSSTLG GVEVRNVRYS
120 LKQLQSAMEQ LDAGANARVK GVSKPLDGVQ SWYVDPRSNA VVVKVDDGAT EAGVDFVALS
180 GADSAQVRIE SSPGKLQTTA NIVGGIEYSI NNASLCSVGF SVTRGATKGF VTAGHCGTVN
240 ATARIGGAVV GTFAARVFPG NDRAWVSLTS AQTLLPRVAN GSSFVTVRGS TEAAVGAAVC
300 RSGRTTGYQC GTITAKNVTA NYAEGAVRGL TQGNACMGRG DSGGSWITSA GQAQGVMSGG
360 NVQSNGNNCG IPASQRSSLF ERLQPILSQY GLSLVTG
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
78391
Epstein D.M.,Wensink P.C.
The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes.
J. Biol. Chem.
263
16586-16590
1988
78393
Silen J.L.,McGrath C.N.,Smith K.R.,Agard D.A.
Molecular analysis of the gene encoding alpha-lytic protease: evidence for a preproenzyme.
Gene
69
237-244
1988
78394
Olson M.O.J.,Nagabhushan N.,Dzwiniel M.,Smillie L.B.,Whitaker D.R.
Priaary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases.
Nature
228
438-442
1970
78395
Brayer G.D.,Delbaere L.T.J.,James M.N.G.
Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8-A resolution.
J. Mol. Biol.
131
743-775
1979
78396
Fujinaga M.,Delbaere L.T.J.,Brayer G.D.,James M.N.G.
Refined structure of alpha-lytic protease at 1.7-A resolution. Analysis of hydrogen bonding and solvent structure.
J. Mol. Biol.
184
479-502
1985
78397
Peters R.J.,Shiau A.K.,Sohl J.L.,Anderson D.E.,Tang G.,Silen J.L.,Agard D.A.
Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.
Biochemistry
37
12058-12067
1998
78398
Sauter N.K.,Mau T.,Rader S.D.,Agard D.A.
Structure of alpha-lytic protease complexed with its pro region.
Nat. Struct. Biol.
5
945-950
1998