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Abz-Ala-Ala-Phe-4-nitroanilide + H2O
Abz-Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
acetyl-Ala-Pro-Ala-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
Staphylococcus aureus peptidoglycan + H2O
?
the enzyme possesses a Gly-Gly endopeptidase activity with respect to staphylococcal peptidoglycan and an amidase that manifests an N-acetylmuramoyl-L-Ala amidase activity with respect to this substrate
-
-
?
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide
?
-
-
-
?
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Ala + 4-nitroaniline
-
high activity with wild-type enzyme and mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
weak activity with wild-type enzyme, high activity with mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
weak activity with wild-type enzyme, high activity with mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
high activity with wild-type enzyme and mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-X-p-nitroanilide + H2O
?
-
X: Gly, Thr, Val, Leu, Ile, Met, Phe
-
-
?
succinyl-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
?
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin + H2O
?
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
peptidoglycan + H2O
?
-
-
-
-
?
additional information
?
-
-
oligopeptides on the carbonyl side of amino acids with short neutral aliphatic side-chains
-
-
?
additional information
?
-
-
carbonyl end of small residues as Val, Ser, Val
-
-
?
additional information
?
-
-
preferential cleavage of bonds adjacent to L-alanine
-
-
?
additional information
?
-
-
carbonyl end of small residues as Val, Ser, Val
-
-
?
additional information
?
-
-
preferential cleavage of bonds adjacent to L-alanine
-
-
?
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Anemia, Diamond-Blackfan
Identification of mutations in the ribosomal protein L5 (RPL5) and ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan anemia.
Anemia, Diamond-Blackfan
Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients.
Budd-Chiari Syndrome
Identification of RPL5 gene variants and the risk of hepatic vein thrombosis in Saudi patients.
Cholestasis
Abnormal lipoproteins in a case of primary biliary cirrhosis.
Cleft Palate
Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients.
Congenital Microtia
The important role of RPS14, RPL5 and MDM2 in TP53-associated ribosome stress in mycophenolic acid-induced microtia.
Infections
Investigating the Existence of Ribosomal Protein L5 Gene in Syrian Strain of Leishmania tropica Genome: Sequencing It and Evaluating Its Immune Response as DNA Vaccine.
Infections
Potato spindle tuber viroid modulates its replication through a direct interaction with a splicing regulator.
Liver Neoplasms
Colocalization of MID1IP1 and c-Myc is Critically Involved in Liver Cancer Growth via Regulation of Ribosomal Protein L5 and L11 and CNOT2.
Lung Neoplasms
Ribosomal protein L5 mediated inhibition of c-Myc is critically involved in sanggenon G induced apoptosis in non-small lung cancer cells.
Muscular Diseases
Stable reference genes for expression studies in breast muscle of normal and white striping-affected chickens.
Neoplasms
Analysis of the Antiproliferative Effect of Ankaferd Hemostat on Caco-2 Colon Cancer Cells via LC/MS Shotgun Proteomics Approach.
Neoplasms
The important role of RPS14, RPL5 and MDM2 in TP53-associated ribosome stress in mycophenolic acid-induced microtia.
Sarcoma, Avian
Engineering proteases with altered specificity.
Teratocarcinoma
p53 and the ribosomal protein L5 participate in high molecular mass complex formation with protein kinase CK2 in murine teratocarcinoma cell line F9 after serum stimulation and cisplatin treatment.
Thrombosis
Identification of RPL5 gene variants and the risk of hepatic vein thrombosis in Saudi patients.
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G216A
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216F
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216G
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216H
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216I
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216L
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216Q
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216S
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216T
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216V
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216W
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216Y
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
additional information
-
Pro region N-domain mutants: disruption of the hydrogen bonding potentials of Y26 and E30 primarily alters Pro binding to the folding transition state as compared to binding in the initial and native state complexes
M190A
-
active site mutant
M190A
-
mutation broadens specificity while maintaining or increasing catalytic activity
M190A
-
active site mutant
-
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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.
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda