3.4.21.12: alpha-lytic endopeptidase
This is an abbreviated version!
For detailed information about alpha-lytic endopeptidase, go to the full flat file.
Word Map on EC 3.4.21.12
Reaction
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins =
Synonyms
ALP, Alpha-lytic endopeptidase, alpha-lytic protease, alpha-lytic proteinase, alphaLP, bacteriolytic protease L5, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase, Myxobacter alpha-lytic proteinase, protein L5, proteinase, Mycobacterium sorangium alpha-lytic, proteinase, Myxobacter alpha-lytic
ECTree
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Reference on EC 3.4.21.12 - alpha-lytic endopeptidase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bone, R.; Shenvi, A.B.; Kettner, C.A.; Agard, D.A.
Serine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid
Biochemistry
26
7609-7614
1987
Lysobacter enzymogenes
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
Lysobacter enzymogenes
Bachovchin, W.W.; Kaiser, R.; Richards, J.H.; Roberts, J.D.
Catalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease
Proc. Natl. Acad. Sci. USA
78
7323-7326
1981
Lysobacter enzymogenes
Brayer, G.D.; delBaere, L.T.J.; James, M.N.G.
Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8 Angstroms resolution
J. Mol. Biol.
131
743-775
1979
unidentified myxobacterium, unidentified myxobacterium 495
delBaere, L.T.J.; Brayer, G.D.; James, M.N.G.
Comparison of the predicted model of alpha-lytic protease with the x-ray structure
Nature
279
165-168
1979
unidentified myxobacterium, unidentified myxobacterium 495
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
unidentified myxobacterium, unidentified myxobacterium 495
Davis, J.H.; Agard, D.A.
Relationship between enzyme specificity and the backbone dynamics of free and inhibited alpha-lytic protease
Biochemistry
37
7696-7707
1998
Lysobacter enzymogenes
Sohl, J.L.; Shiau, A.K.; Rader, S.D.; Wilk, B.J.; Agard, D.A.
Inhibition of alpha-lytic protease by pro region C-terminal steric occlusion of the active site
Biochemistry
36
3894-3902
1997
Lysobacter enzymogenes
Mace, J.E.; Agard, D.A.
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity
J. Mol. Biol.
254
720-736
1995
Lysobacter enzymogenes
Bone, R.; Sampson, N.S.; Bartlett, P.A.; Agard, D.A.
Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters
Biochemistry
30
2263-2272
1991
Lysobacter enzymogenes
Li, S.; Norioka, S.; Sakiyama, F.
Purification, staphylolytic activity, and cleavage sites of alpha-lytic protease from Achromobacter lyticus
J. Biochem.
122
772-778
1997
Achromobacter lyticus, Achromobacter lyticus M497-1
Ivanov, D.; Bachovchin, W.W.; Redfield, A.G.
Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease
Biochemistry
41
1587-1590
2002
Lysobacter enzymogenes
Cunningham, E.L.; Mau, T.; Truhlar, S.M.; Agard, D.A.
The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding
Biochemistry
41
8860-8867
2002
Lysobacter enzymogenes
Fuhrmann, C.N.; Kelch, B.A.; Ota, N.; Agard, D.A.
The 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain
J. Mol. Biol.
338
999-1013
2004
Lysobacter enzymogenes (P00778)
Derman, A.I.; Agard, D.A.
Two energetically disparate folding pathways of alpha-lytic protease share a single transition state
Nat. Struct. Biol.
7
394-397
2000
Lysobacter enzymogenes
Ota, N.; Agard, D.A.
Enzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions
Protein Sci.
10
1403-1414
2001
Lysobacter enzymogenes
Muranova, T.A.; Krasovskaya, L.A.; Tsfasman, I.M.; Stepnaya, O.A.; Kulaev, I.S.
Structural investigations and identification of the extracellular bacteriolytic endopeptidase L1 from Lysobacter sp. XL1
Biochemistry
69
501-505
2004
Lysobacter sp.
Fuhrmann, C.N.; Daugherty, M.D.; Agard, D.A.
Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis
J. Am. Chem. Soc.
128
9086-9102
2006
Lysobacter enzymogenes (P00778)
Haddad, K.C.; Sudmeier, J.L.; Bachovchin, D.A.; Bachovchin, W.W.
alpha-Lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities
Proc. Natl. Acad. Sci. USA
102
1006-1011
2005
Lysobacter enzymogenes
Qasim, M.A.; Van Etten, R.L.; Yeh, T.; Saunders, C.; Ganz, P.J.; Qasim, S.; Wang, L.; Laskowski, M.
Despite having a common P1 Leu, eglin C inhibits alpha-lytic proteinase a million-fold more strongly than does turkey ovomucoid third domain
Biochemistry
45
11342-11348
2006
Lysobacter enzymogenes (P00778)
Deng, N.J.; Cieplak, P.
Insights into affinity and specificity in the complexes of alpha-lytic protease and its inhibitor proteins: binding free energy from molecular dynamics simulation
Phys. Chem. Chem. Phys.
11
4968-4981
2009
Lysobacter enzymogenes (P00778)
Salimi, N.L.; Ho, B.; Agard, D.A.
Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic protease
PLoS Comput. Biol.
6
e1000689
2010
Lysobacter enzymogenes
Meyer, J.G.; Kim, S.; Maltby, D.A.; Ghassemian, M.; Bandeira, N.; Komives, E.A.
Expanding proteome coverage with orthogonal-specificity alpha-lytic proteases
Mol. Cell. Proteomics
13
823-835
2014
Lysobacter enzymogenes, Lysobacter enzymogenes 495
Kudryakova, I.V.; Gabdulkhakov, A.G.; Tishchenko, S.V.; Lysanskaya, V.Y.; Suzina, N.E.; Tsfasman, I.M.; Afoshin, A.S.; Vasilyeva, N.V.
Structural and functional properties of antimicrobial protein L5 of Lysobacter sp. XL1
Appl. Microbiol. Biotechnol.
102
10043-10053
2018
Lysobacter sp. XL1 (D2K8B4)
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