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Information on EC 3.4.17.2 - carboxypeptidase B and Organism(s) Homo sapiens and UniProt Accession P15086

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.2 carboxypeptidase B
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This record set is specific for:
Homo sapiens
UNIPROT: P15086 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
preferential release of a C-terminal lysine or arginine amino acid
Synonyms
cpb, carboxypeptidase b, basic carboxypeptidase, pancreas-specific protein, carboxypeptidase b1, b carboxypeptidase, ppcpb, hbcpb, cpbag1, cpbas1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
B carboxypeptidase
-
47 kDa zymogen granule membrane associated protein
-
-
-
-
aCAP
-
-
basic carboxypeptidase
-
-
carboxypeptidase B
-
-
carboxypeptidase BII
-
-
-
-
HBCPB
-
-
Pancreas-specific protein
-
-
-
-
PASP
-
-
-
-
PcpB
-
-
protaminase
TAFI
-
possesses carboxypeptidase B-like activity
thrombin-activatable fibrinolysis inhibitor
thrombin-activatable procarboxypeptidase B
-
-
tissue carboxypeptidase B
-
-
ZAP47
-
-
-
-
additional information
-
the enzyme belongs to the M14A peptidase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential release of a C-terminal lysine or arginine amino acid
show the reaction diagram
conserved catalytic residues are Glu270 and Asp127, residues Ser207, Glu243, and Asp255 determine the substrate specificity
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-24-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-(2-furyl)acryloyl-L-Ala-L-Arg + H2O
3-(2-furyl)acryloyl-L-Ala + L-Arg
show the reaction diagram
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
-
-
-
-
?
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR + H2O
biotin-(epsilon-aminocaproic acid)2-GLMVGGVV + Arg
show the reaction diagram
-
-
-
?
endostar + H2O
?
show the reaction diagram
-
endostar is a derivative of human endostatin that is modified with an additional metal-chelating sequence at the N-terminus. A mixture of carboxypeptidase A and carboxypeptidase B is applied to catalyse the hydrolysis of the C-terminus of apo and holo endostar
-
-
?
hippuryl-L-Arg
hippuric acid + L-Arg
show the reaction diagram
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
-
?
hippuryl-L-Asp + H2O
hippuric acid + L-aspartate
show the reaction diagram
-
hydrolyzed by mutant enzyme D253K and mutant enzyme D253R, wild type enzyme shows no activity
-
-
?
hippuryl-L-Glu + H2O
hippuric acid + Glu
show the reaction diagram
-
hydrolyzed by mutant enzyme D253K, wild type enzyme shows no activity
-
-
?
hippuryl-Lys + H2O
hippuric acid + Lys
show the reaction diagram
insulin-like peptide 5 precursor + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Arg-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
OPN-R + H2O
OPN-L + ?
show the reaction diagram
-
osteopontin (OPN) gets activated by thrombin resulting in OPN-R. OPN-R is subsequently inactivated by CPB generating OPN-L
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
OPN-R + H2O
OPN-L + ?
show the reaction diagram
-
osteopontin (OPN) gets activated by thrombin resulting in OPN-R. OPN-R is subsequently inactivated by CPB generating OPN-L
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
-
required
Co2+
-
CoCl2, accelerates hydrolysis of hippuryl-L-Arg and hippuryl-Lys
Zinc
-
0.96 gatom of zinc per mol of enzyme
Zn2+
-
1 mol Zn2+ per mol of enzyme, coordinated by the conserved residues His69, Glu72, and His196
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tick carboxypeptidase inhibitor
TCI, from Rhipicephalus bursa, recombinantly expressd in Escherichia coli strain BL21(DE3) periplasm and purification by cation exchange and adsorption chromatography, binding structure at the active site, overview
-
(DL-5-guanidinoethyl)mercaptosuccinic acid
-
-
1,10-phenanthroline
-
-
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
-
2-Guanidinoethylmercaptosuccinic acid
-
-
2-mercaptomethyl-3-guanidinoethyl-propanoic acid
-
-
2-mercaptomethyl-5-guanidinopentanoic acid
-
-
6-amino-n-hexanoic acid
-
-
antithrombomodulin antibody
-
-
-
Co2+
-
hydrolysis of hippuryl-L-Arg
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
DL-benzylsuccinic acid
-
-
DL-guanidinoethylmercaptosuccinic acid
-
-
epsilon-aminocaproic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
leech carboxypeptidase inhibitor
-
-
-
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
-
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
-
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
-
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
-
methyl N-[[(1R,2S)-2-([N-[(benzyloxy)carbonyl]-beta-alanyl]amino)cyclobutyl]carbonyl]-beta-alaninate
-
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
-
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
-
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
-
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
-
N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
-
potato carboxypeptidase inhibitor
-
protamine
-
-
tick carboxypeptidase inhibitor
-
TCI, from the ixodid tick Rhipicephalus bursa, recombinant expression in Escherichia coli, DNA and amino acid sequence determination and analysis, binding structure and inhibition mechanism, overview
-
Urea
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thrombin
-
-
-
Thrombomodulin
-
HT1080 cells mediate activation of TAFI in plasma in the presence of soluble-type thrombomodulin through cell-dependent prothrombin activation. HT1080 cells stably expressing thrombomodulin mediate plasma TAFI activation without added soluble thrombomodulin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
3-(2-furyl)acryloyl-L-Ala-L-Arg
-
-
0.008
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
-
pH 7.4
0.277 - 0.31
hippuryl-Arg
0.05 - 0.19
hippuryl-L-Arg
0.06
N-(4-methoxyphenylazoformyl)-Arg
-
-
additional information
additional information
-
Km-values of mutant enzymes with hippuryl-Glu as substrate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9
biotin-(epsilon-aminocaproic acid)2-GLMVGGVVR
-
pH 7.4
61
hippuryl-Arg
-
-
0.16 - 0.26
hippuryl-Asp
3.8
hippuryl-Glu
-
mutant enzyme D253K
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075
1-(4-chlorophenyl)-2-(5-(2-hydroxyphenyl)-1,3,4-oxadiazol-2-ylthio)ethanone
-
pH 7.5
0.00005
2-Guanidinoethylmercaptosuccinic acid
-
pH 7.4
0.0000082
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
pH 7.4
0.01
DL-benzylsuccinic acid
-
pH 7.5
0.0011
DL-guanidinoethylmercaptosuccinic acid
-
pH 7.5
0.9
epsilon-aminocaproic acid
-
pH 7.4
0.0074
isopropyl 2-(4-benzyl-5-(2-methoxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.275
methyl (1R,2S)-2-([[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22°C
0.07
methyl (1S,2R)-2-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)cyclobutanecarboxylate
-
pH 7.5, 22°C
0.0049
methyl 2-(4-benzyl-5-(2-hydroxyphenyl)-4H-1,2,4-triazol-3-ylthio)acetate
-
pH 7.5
0.41
methyl 5-([[(1S,2R)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]amino)pentanoate
-
pH 7.5, 22°C
0.165
methyl N-[[(1R,2S)-2-([N-[(benzyloxy)carbonyl]-beta-alanyl]amino)cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.4
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.5
methyl N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]glycinate
-
pH 7.5, 22°C
0.0012
N-(3-chlorophenyl)-4-((5-((3-methoxybenzyl)thio)-1,3,4-oxadiazol-2-yl)methyl)thiazol-2-amine
-
pH 7.5
0.0045
N-benzyl-N-(4-phenylthiazol-2-yl)cyclopropanecarboxamide
-
pH 7.5
0.043
N-[[(1R,2S)-2-[[(benzyloxy)carbonyl]amino]cyclobutyl]carbonyl]-beta-alaninate
-
pH 7.5, 22°C
0.000001 - 0.0000018
potato carboxypeptidase inhibitor
-
0.01
protamine
-
above, pH 7.4
0.0000013
tick carboxypeptidase inhibitor
-
pH 7.4, 23°C
-
additional information
additional information
-
the Ki values for 2-mercaptomethyl-3-guanidinoethyl-propanoic acid, potato and leech carboxypeptidase inhibitors, and 2-mercaptomethyl-5-guanidinopentanoic acid are in the nanomolar range
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1192
-
carboxypeptidase B II
862
-
carboxypeptidase B I
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
hydrolysis of hippuryl-L-Arg
7
-
cleavage of hippuryl-L-Arg
7.4
-
assay at
7.5
-
assay at
7.5 - 7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6: about 60% of maximal activity with carboxypeptidase B I, about 50% of maximal activity with carboxypeptidase B II, pH 10: about 70% of maximal activity with carboxypeptidase B I, about 60% of maximal activity with carboxypeptidase B II, cleavage of hippuryl-L-Arg
7 - 10.5
-
pH 7: about 45% of maximal activity with carboxypeptidase B I, about 30% of maximal activity with carboxypeptidase B II, pH: 10.5: about 90% of maximal activity with carboxypeptidase B I, about 80% of maximal activity with carboxypeptidase B II, hydrolysis of hippuryl-L-Arg
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
25
-
assay at
30
-
assay at
37
-
assay at
additional information
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
majority of the enzyme exists in the prepro-form
Manually annotated by BRENDA team
-
in synovial fluids from osteoarthritis patients, high levels of proCPB are associated with high levels of proinflammatory cytokines and complement components, and levels of proCPB correlated positively with those of membrane attack complex (MAC)
Manually annotated by BRENDA team
-
fibroblast-like synoviocytes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
Cpb2 knockout mice develop greater cartilage damage than wild-type mice and have a greater number of osteophytes and degree of synovitis
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CBPB1_HUMAN
417
0
47368
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23500
27700
-
gel filtration
32210
-
carboxypeptidase B II, gel filtration
32920
-
carboxypeptidase B I, gel filtration
34000
-
1 * 34000, carboxypeptidase B, SDS-PAGE
35000
-
SDS-PAGE, activated form
58000
-
SDS-PAGE
65000
-
Western blot analysis
additional information
-
analysis of active enzyme and inactive proenzyme by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
-
1 * 34000, carboxypeptidase B, SDS-PAGE
additional information
-
the pancreatic enzyme is divided in the activation domain and the enzyme domain linked by a connecting region
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
cleavage and activation of the recombinant zymogen by trypsin
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme in complex with tick carboxypeptidase inhibitor, sitting drop vapour diffusion method, mixing of equal volumes of protein and reservoir solutions, the latter containing 0.1 M bis-Tris. pH 5.5, 0.2 M lithium sulfate monohydrate, and 25% w/v PEG 3350, a few weeks at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D253K
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. Activity with hippuryl-Glu and hippuryl-Asp, this activity is reduced hundred-fold compared with the native enzyme with hippuryl-Arg as substrate
D253R
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. Activity with hippuryl-Glu and hippuryl-Asp, this activity is reduced hundred-fold compared with the native enzyme with hippuryl-Arg as substrate
G251T/D253K
-
the mutant enzyme is unable to hydrolyze hippuryl-Arg. 100times more active against hippuryl-L-Glu as substrate than the single mutant D253K
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native proenzyme from pancreatic juice, separation of active enzyme and inactive proenzyme by gel filtration
-
purified by chromatography on Q-Sepharose Fast Flow, Heparin-Sepharose CL-6B, Sephacryl S-300, and plasminogen-Sepharose columns
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the zymogen in Pichia pastoris straim KM71
DNA sequence determination, phylogenetic tree
-
recombinantly expressed
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in synovial fluids from osteoarthritis patients CPB expression is up-regulated
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for design of active site inhibitors based on the structure of tick carboxypeptidase inhibitor, a potential antithrombolytic drug
diagnostics
-
the enzyme is a serum marker for acute pancreatitis and pancreatic graft injection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakharov, D.V.; Plow, E.F.; Rijken, D.C.
On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
J. Biol. Chem.
272
14477-14482
1997
Homo sapiens
Manually annotated by BRENDA team
Eaton, D.L.; Malloy, B.E.; Tsai, S.P.; Henzel, W.; Drayna, D.
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
J. Biol. Chem.
266
21833-21838
1991
Homo sapiens
Manually annotated by BRENDA team
Geokas, M.C.; Largman, C.; Brodrick, J.W.; Raeburn, S.; Rinderknecht, H.
Human pancreatic carboxypeptidase B. I. Isolation, purification, and characterization of fraction II
Biochim. Biophys. Acta
391
396-402
1975
Homo sapiens
Manually annotated by BRENDA team
Brodrick, J.W.; Geokas, M.C.; Largman, C.
Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion
Biochim. Biophys. Acta
452
468-481
1976
Homo sapiens
Manually annotated by BRENDA team
Marinkovic, D.V.; Marinkovic, J.N.; Erds, E.G.; Robinson, C.J.G.
Purification of carboxypeptidase B from human pancreas
Biochem. J.
163
253-260
1977
Homo sapiens
Manually annotated by BRENDA team
Valnickova, Z.; Thogersen, I.B.; Christensen, S.; Chu, C.T.; Pizzo, S.V.; Enghild, J.J.
Activated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone protein
J. Biol. Chem.
371
12937-12943
1996
Homo sapiens
Manually annotated by BRENDA team
Edge, M.; Forder, C.; Hennam, J.; Lee, I.; Tonge, D.; Hardern, I.; Fitton, J.; Eckersley, K.; East, S.; Shufflebotham, A.; Blakey, D.; Slater, A.
Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants
Protein Eng.
11
1229-1234
1998
Homo sapiens
Manually annotated by BRENDA team
Mao, S.S.; Colussi, D.; Bailey, C.M.; Bosserman, M.; Burlein, C.; Gardell, S.J.; Carroll, S.S.
Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor
Anal. Biochem.
319
159-170
2003
Homo sapiens
Manually annotated by BRENDA team
Matsumoto, A.; Motozaki, K.; Seki, T.; Sasaki, R.; Kawabe, T.
Expression of human brain carboxypeptidase B, a possible cleaving enzyme for beta-amyloid precursor protein, in peripheral fluids
Neurosci. Res.
39
313-317
2001
Homo sapiens
Manually annotated by BRENDA team
Aviles, F.X.; Vendrell, J.
Carboxypeptidase B
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press
2
831-833
2004
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Arolas, J.L.; Lorenzo, J.; Rovira, A.; Castella, J.; Aviles, F.X.; Sommerhoff, C.P.
A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization
J. Biol. Chem.
280
3441-3448
2005
Homo sapiens
Manually annotated by BRENDA team
Arolas, J.L.; Popowicz, G.M.; Lorenzo, J.; Sommerhoff, C.P.; Huber, R.; Aviles, F.X.; Holak, T.A.
The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
J. Mol. Biol.
350
489-498
2005
Homo sapiens (P15086), Homo sapiens
Manually annotated by BRENDA team
Borgstroem, A.; Regner, S.
Active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
Pancreatology
5
530-536
2005
Homo sapiens
Manually annotated by BRENDA team
Higuchi, T.; Nakamura, T.; Kakutani, H.; Ishii, H.
Thrombomodulin suppresses invasiveness of HT1080 tumor cells by reducing plasminogen activation on the cell surface through activation of thrombin-activatable fibrinolysis inhibitor
Biol. Pharm. Bull.
32
179-185
2009
Homo sapiens
Manually annotated by BRENDA team
Luo, X.; Bathgate, R.A.; Zhang, W.J.; Liu, Y.L.; Shao, X.X.; Wade, J.D.; Guo, Z.Y.
Design and recombinant expression of insulin-like peptide 5 precursors and the preparation of mature human INSL5
Amino Acids
39
1343-1352
2010
Homo sapiens
Manually annotated by BRENDA team
Sharif, S.A.; Du, X.; Myles, T.; Song, J.J.; Price, E.; Lee, D.M.; Goodman, S.B.; Nagashima, M.; Morser, J.; Robinson, W.H.; Leung, L.L.
Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis
Arthritis Rheum.
60
2902-2912
2009
Homo sapiens
Manually annotated by BRENDA team
Fernandez, D.; Torres, E.; Aviles, F.X.; Ortuno, R.M.; Vendrell, J.
Cyclobutane-containing peptides: evaluation as novel metallocarboxypeptidase inhibitors and modelling of their mode of action
Bioorg. Med. Chem.
17
3824-3828
2009
Homo sapiens
Manually annotated by BRENDA team
Jiang, L.P.; Zou, C.; Yuan, X.; Luo, W.; Wen, Y.; Chen, Y.
N-terminal modification increases the stability of the recombinant human endostatin in vitro
Biotechnol. Appl. Biochem.
54
113-120
2009
Homo sapiens
Manually annotated by BRENDA team
Fernandez, D.; Aviles, F.X.; Vendrell, J.
A new type of five-membered heterocyclic inhibitors of basic metallocarboxypeptidases
Eur. J. Med. Chem.
44
3266-3271
2009
Helicoverpa zea, Homo sapiens
Manually annotated by BRENDA team
Lepus, C.; Song, J.; Wang, Q.; Wagner, C.; Lindstrom, T.; Chu, C.; Sokolove, J.; Leung, L.; Robinson, W.
Carboxypeptidase B serves as a protective mediator in osteoarthritis
Arthritis Rheum.
66
101-106
2014
Homo sapiens, Mus musculus
Manually annotated by BRENDA team