EzCatDB: D00528
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DB codeD00528
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.119

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

P36368
Protein nameEpidermal growth factor-binding protein type Bkallikrein 13
KLK13
kallikrein mK13
mGK-13
mK13
mKLK13
prorenin converting enzyme 1
PRECE-1
prorenin-converting enzyme
PRECE
proteinase P
SynonymsEGF-BP B
EC 3.4.21.119
Glandular kallikrein K13
mGK-13
Tissue kallikrein 13
Prorenin-converting enzyme 1
PRECE-1
RefSeqNP_034245.3 (Protein)
NM_010115.6 (DNA/RNA sequence)
PfamPF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP36368
Entry nameEGFB2_MOUSE
ActivityHydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idL00034C00001L00035L00036I00087I00085I00086
CompoundProreninH2OReninLys-ArgPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typeamide group,amine group,imine group,lipid,peptide/proteinH2Opeptide/proteinamide group,amine group,imine group,lipid,peptide/protein


ChEBI
15377

74553



PubChem
962
22247451

15061422



               
1ao5A01Unbound UnboundUnboundUnboundUnboundUnbound
1ao5B01Unbound UnboundUnboundUnboundUnboundUnbound
1ao5A02Unbound UnboundUnboundUnboundUnboundUnbound
1ao5B02Unbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbCatalytic residuesMain-chain involved in catalysis
          
1ao5A01SER 195
ASP 193;SER 195
1ao5B01SER 195
ASP 193;SER 195
1ao5A02HIS 57;ASP 102 
 
1ao5B02HIS 57;ASP 102 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]

[13]Scheme 3, Scheme 10, Scheme 11, p.94-104
[14]p.2039
[21]p.258-259
[29]p.27277-27278
[30]p.329-332

references
[1]
CommentsREVIEW.
Medline ID82194877
PubMed ID7043199
JournalMethods Enzymol
Year1981
Volume80 Pt C
Pages493-532
AuthorsFiedler F, Fink E, Tschesche H, Fritz H
TitlePorcine glandular kallikreins.
Related UniProtKBP00752
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2 ANGSTROMS), AND REVISIONS.
Medline ID83189107
PubMed ID6551452
JournalJ Mol Biol
Year1983
Volume164
Pages237-82
AuthorsBode W, Chen Z, Bartels K, Kutzbach C, Schmidt-Kastner G, Bartunik H
TitleRefined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin.
Related PDB2pka
Related UniProtKBP00752
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH BOVINE PANCREATIC TRYPSIN INHIBITOR.
Medline ID83189108
PubMed ID6188842
JournalJ Mol Biol
Year1983
Volume164
Pages283-311
AuthorsChen Z, Bode W
TitleRefined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex.
Related PDB2kai
Related UniProtKBP00752
[4]
PubMed ID2954262
JournalThromb Res
Year1987
Volume45
Pages451-62
AuthorsHijikata-Okunomiya A, Okamoto S, Kikumoto R, Tamao Y, Ohkubo K, Tezuka T, Tonomura S, Matsumoto O
TitleSimilarity and dissimilarity in the stereogeometry of the active sites of thrombin, trypsin, plasmin and glandular kallikrein.
[5]
CommentsSTRUCTURE OF CARBOHYDRATES.
Medline ID89062455
PubMed ID3196708
JournalBiochemistry
Year1988
Volume27
Pages7146-54
AuthorsTomiya N, Yamaguchi T, Awaya J, Kurono M, Endo S, Arata Y, Takahashi N, Ishihara H, Mori M, Tejima S
TitleStructural analyses of asparagine-linked oligosaccharides of porcine pancreatic kallikrein.
Related UniProtKBP00752
[6]
PubMed ID2012805
JournalBiochemistry
Year1991
Volume30
Pages3443-50
AuthorsFahnestock M, Woo JE, Lopez GA, Snow J, Walz DA, Arici MJ, Mobley WC
Titlebeta-NGF-endopeptidase: structure and activity of a kallikrein encoded by the gene mGK-22.
[7]
PubMed ID1868047
JournalBiochemistry
Year1991
Volume30
Pages7666-72
AuthorsHatala MA, DiPippo VA, Powers CA
TitleBiological thiols elicit prolactin proteolysis by glandular kallikrein and permit regulation by biochemical pathways linked to redox control.
[8]
PubMed ID1507198
JournalJ Med Chem
Year1992
Volume35
Pages3094-102
AuthorsDeshpande MS, Burton J
TitleMapping the binding site of tissue kallikrein: preparation and testing of all possible substrate analog inhibitors homologous with the sequence of kininogen between Ser386 and Gln392.
[9]
PubMed ID8148470
JournalDrug Des Discov
Year1993
Volume10
Pages297-317
AuthorsBarth A, Wahab M, Brandt W, Frost K
TitleClassification of serine proteases derived from steric comparisons of their active sites.
[10]
PubMed ID8254673
JournalJ Mol Biol
Year1993
Volume234
Pages779-815
AuthorsSali A, Blundell TL
TitleComparative protein modelling by satisfaction of spatial restraints.
[11]
PubMed ID7526861
JournalBiochem Biophys Res Commun
Year1994
Volume204
Pages1251-6
AuthorsVihinen M
TitleModeling of prostate specific antigen and human glandular kallikrein structures.
[12]
PubMed ID7749384
JournalBraz J Med Biol Res
Year1994
Volume27
Pages1935-42
AuthorsSueiras-Diaz J, Jones DM, Ashworth D, Horton J, Evans DM, Szelke M
TitleCleavage of human kininogen fragments at Met-Lys by human tissue kallikrein.
[13]
PubMed ID9116171
JournalDrug Des Discov
Year1994
Volume12
Pages89-111
AuthorsBarth A, Frost K, Wahab M, Brandt W, Schadler HD, Franke R
TitleClassification of serine proteases derived from steric comparisons of their active sites, part II: "Ser, His, Asp arrangements in proteolytic and nonproteolytic proteins".
[14]
PubMed ID7535613
JournalProtein Sci
Year1994
Volume3
Pages2033-44
AuthorsVilloutreix BO, Getzoff ED, Griffin JH
TitleA structural model for the prostate disease marker, human prostate-specific antigen.
[15]
PubMed ID7864830
JournalBiochem J
Year1995
Volume306
Pages63-9
AuthorsChagas JR, Portaro FC, Hirata IY, Almeida PC, Juliano MA, Juliano L, Prado ES
TitleDeterminants of the unusual cleavage specificity of lysyl-bradykinin-releasing kallikreins.
[16]
PubMed ID7538242
JournalUrology
Year1995
Volume45
Pages801-6
AuthorsBridon DP, Dowell BL
TitleStructural comparison of prostate-specific antigen and human glandular kallikrein using molecular modeling.
[17]
PubMed ID8961351
JournalProtein Eng
Year1996
Volume9
Pages987-95
AuthorsMoreau T, Gauthier F
TitleHomology modelling of rat kallikrein rK9, a member of the tissue kallikrein family: implications for substrate specificity and inhibitor binding.
[18]
PubMed ID9208936
JournalEur J Biochem
Year1997
Volume246
Pages440-6
AuthorsMikolajczyk SD, Millar LS, Marker KM, Grauer LS, Goel A, Cass MM, Kumar A, Saedi MS
TitleAla217 is important for the catalytic function and autoactivation of prostate-specific human kallikrein 2.
[19]
PubMed ID9491347
JournalJ Comput Aided Mol Des
Year1997
Volume11
Pages547-56
AuthorsHenriques EF, Ramos MJ, Reynolds CA
TitleInclusion of conserved buried water molecules in the model structure of rat submaxillary kallikrein.
[20]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID97376615
PubMed ID9232643
JournalProtein Sci
Year1997
Volume6
Pages1418-25
AuthorsTimm DE
TitleThe crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme).
Related PDB1ao5
Related UniProtKBP36368
[21]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH HIRUSTASIN.
Medline ID97184690
PubMed ID9032072
JournalStructure
Year1997
Volume5
Pages253-64
AuthorsMittl PR, Di Marco S, Fendrich G, Pohlig G, Heim J, Sommerhoff C, Fritz H, Priestle JP, Grutter MG
TitleA new structural class of serine protease inhibitors revealed by the structure of the hirustasin-kallikrein complex.
Related PDB1hia
Related UniProtKBP00752
[22]
PubMed ID9568894
JournalProtein Sci
Year1998
Volume7
Pages875-85
AuthorsKatz BA, Liu B, Barnes M, Springman EB
TitleCrystal structure of recombinant human tissue kallikrein at 2.0 A resolution.
[23]
PubMed ID9521101
JournalProtein Sci
Year1998
Volume7
Pages259-69
AuthorsPiironen T, Villoutreix BO, Becker C, Hollingsworth K, Vihinen M, Bridon D, Qiu X, Rapp J, Dowell B, Lovgren T, Pettersson K, Lilja H
TitleDetermination and analysis of antigenic epitopes of prostate specific antigen (PSA) and human glandular kallikrein 2 (hK2) using synthetic peptides and computer modeling.
[24]
PubMed ID9933620
JournalJ Biol Chem
Year1999
Volume274
Pages4220-4
AuthorsKishi T, Kato M, Shimizu T, Kato K, Matsumoto K, Yoshida S, Shiosaka S, Hakoshima T
TitleCrystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.
[25]
PubMed ID10195448
JournalJ Pept Res
Year1999
Volume53
Pages109-19
AuthorsJuliano MA, Filira F, Gobbo M, Rocchi R, Del Nery E, Juliano L
TitleChromogenic and fluorogenic glycosylated and acetylglycosylated peptides as substrates for serine, thiol and aspartyl proteases.
[26]
PubMed ID10993887
JournalJ Biol Chem
Year2000
Volume275
Pages38457-66
AuthorsChen VC, Chao L, Chao J
TitleRoles of the P1, P2, and P3 residues in determining inhibitory specificity of kallistatin toward human tissue kallikrein.
[27]
PubMed ID10991942
JournalJ Biol Chem
Year2000
Volume275
Pages40371-7
AuthorsChen VC, Chao L, Chao J
TitleA positively charged loop on the surface of kallistatin functions to enhance tissue kallikrein inhibition by acting as a secondary binding site for kallikrein.
[28]
PubMed ID11983703
JournalJ Biol Chem
Year2002
Volume277
Pages24562-70
AuthorsBernett MJ, Blaber SI, Scarisbrick IA, Dhanarajan P, Thompson SM, Blaber M
TitleCrystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system.
[29]
PubMed ID12016211
JournalJ Biol Chem
Year2002
Volume277
Pages27273-81
AuthorsGomis-Ruth FX, Bayes A, Sotiropoulou G, Pampalakis G, Tsetsenis T, Villegas V, Aviles FX, Coll M
TitleThe structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family.
[30]
CommentsNUCLEOTIDE SEQUENCE [MRNA] OF 62-252, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 25-261.
PubMed ID12217694
JournalJ Mol Biol
Year2002
Volume322
Pages325-37
AuthorsCarvalho AL, Sanz L, Barettino D, Romero A, Calvete JJ, Romao MJ
TitleCrystal structure of a prostate kallikrein isolated from stallion seminal plasma: a homologue of human PSA.
Related PDB1gvz
Related UniProtKBQ6H321
[31]
CommentsX-ray Diffraction
PubMed ID15651049
JournalProteins
Year2005
Volume58
Pages802-14
AuthorsLaxmikanthan G, Blaber SI, Bernett MJ, Scarisbrick IA, Juliano MA, Blaber M
Title1.70 A X-ray structure of human apo kallikrein 1: structural changes upon peptide inhibitor/substrate binding.
Related PDB1spj

comments
This enzyme belongs to the peptidase family-S1, and closely related to kallikrein (D00212 in EzCatDB).
According to the literature, this enzyme has got a catalytic triad, composed of Ser/His/Asp and an oxyanionhole of mainchain amide groups. Thus, it must have a similar reaction mechanism to that of trypsin (D00197 in EzCatDB).

createdupdated
2006-01-102011-02-21


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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