KEGG   ENZYME: 3.4.21.35
Entry
EC 3.4.21.35                Enzyme                                 
Name
tissue kallikrein;
glandular kallikrein;
pancreatic kallikrein;
submandibular kallikrein;
submaxillary kallikrein;
kidney kallikrein;
urinary kallikrein;
kallikrein;
salivary kallikrein;
kininogenin;
kininogenase;
callicrein;
glumorin;
padreatin;
padutin;
kallidinogenase;
bradykininogenase;
depot-padutin;
urokallikrein;
dilminal D;
onokrein P
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
Reaction(IUBMB)
Preferential cleavage of Arg! bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met! or Leu!. The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg! bonds [5]
Comment
Formed from tissue prokallikrein by activation with trypsin. In peptidase family S1 (trypsin family). A large number of tissue kallikrein-related sequences have been reported for rats [16] and mice [7], though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse gamma-renin (EC 3.4.21.54), submandibular proteinase A [2,15], epidermal growth-factor-binding protein, nerve growth factor gamma-subunit, rat tonin [3,4,9], submaxillary proteinases A and B [10], T-kininogenase [18], kallikreins k7 and k8 [17] and human prostate-specific antigen (gamma-seminoprotein, [6])
History
EC 3.4.21.35 created 1965 as EC 3.4.4.21, transferred 1972 to EC 3.4.21.8, part transferred 1981 to EC 3.4.21.35
Orthology
K01325  tissue kallikrein
Genes
HSA3816(KLK1) 3817(KLK2)
PTR107969791(KLK1) 748637(KLK2)
PPS100967412(KLK2) 100995152(KLK1)
GGO101144843(KLK1)
PON100431610(KLK1) 100432729(KLK2)
NLE115836983(KLK1)
HMH116478138(KLK1)
MCC106994826(KLK1) 719436
MCF102135781
MTHB126943132 126943136
MNI105497139 105497145(KLK1)
CSAB103235100(KLK1) 103235106(KLK2)
CATY105595342(KLK1) 105595344
PANU101004790(KLK1) 101006181
TGE112612653 112613504(KLK2)
MLEU105528940(KLK2) 105528944(KLK1)
RRO104667242(KLK1)
RBB108532416(KLK1)
TFN117091647(KLK1)
PTEH111519950(KLK1) 111547903
CANG105514726(KLK1)
CJC100402463(KLK1) 100402826
SBQ101045013(KLK1) 101045648
CIMI108291947 108291980(KLK1) 108291981
CSYR103274723 103274726
MMUR105865551 105865552 105865567
LCAT123623765(KLK1) 123623766
PCOQ105809263(KLK1) 105809362
OGA100964111 100964738(KLK1)
MMU13646(Klk1b22) 13648(Klk1b9) 16612(Klk1) 16613(Klk1b11) 16616(Klk1b21) 16617(Klk1b24) 16618(Klk1b26) 16619(Klk1b27) 16622(Klk1b5) 16623(Klk1b1) 16624(Klk1b8) 18050(Klk1b3)
MCAL110288052 110288646 110288648 110288829 110297501 110298249 110298250 110298251 110298252 110298253 110298254 110298255 110298258 110298259 110298262 110298268
MPAH110315507 110315664 110315691 110315692 110315693 110318293 110318297 110318311 110318333 110318340 110318349
RNO100361452(Klk1c4) 24523(Klk1) 24594(Klk1b3) 24841(Klk1c2) 292855(Klk1c12) 292858(Klk1c10) 292866(Klk1c8) 292868(Klk1c9) 292872(Klk1c3) 408242(Klk1c6)
MCOC116100493 116100494 116101214 116101215 116101217 116102109 116102113
ANU117715292(Klk1)
MUN110539921 110539925
CGE100754155
MAUA106022386(Klk1)
PROB127213897
PLEU114684323(Klk1) 114684353
MORG121446057(Klk1)
MFOT126488198
AAMP119802928(Klk1)
NGI103743763(Klk1) 103743764
HGL101705888 101719001(Klk1)
CPOC100716976 100717627 100717905(Klk1)
CCAN109683867 109683868 109683884
DORD105994168 105994284(Klk1) 105994289 105994292
DSP122125573 122125633(Klk1) 122125638 122125650
PLOP125338534(Klk1) 125338541 125338543 125368107
NCAR124966706 124967234
MMMA107151706 107151708(Klk1)
OCU100101620
OPI105942447(KLK1)
TUP102489025(KLK1)
GVR103608034(KLK1)
CFA403942(KLK1) 403967(KLK2)
CLUD112645074(KLK1) 112645075
VVP112931184 112931507
VLG121475667 121484807
NPO129500105 129500627
AML100476682 100476932(KLK1) 117799551
UMR103657279(KLK1) 103657282
UAH113247288(KLK1) 113247344
UAR123778021(KLK1) 123778040
ELK111160671 111160724
LLV125089860 125089862
MPUF101690899 101692305(KLK1)
MNP132004729 132005283(KLK1)
MLK131817584(KLK1) 131817591
NVS122913862 122913865(KLK1)
ORO101375682 101382562
EJU114199586(KLK1) 114199592
ZCA113935385(KLK1) 113935397
MLX117997969 117998338(KLK1)
NSU110572972 110572982 110578655 123323730
LWW102751105(KLK1)
FCA101090062(KLK1) 101097936
PYU121018990(KLK1)
PCOO112850833
PBG122493807(KLK1)
PVIV125152590 125152739
LRUF124511698 124511770
PTG102963319(KLK1) 102963589
PPAD109252991 109252996(KLK1)
PUC125916128
AJU106989422 106989668
HHV120241686 120244551(KLK1)
BTA493738(KLK1)
BOM102283027(KLK1)
BIU109571921(KLK1)
BBUB102406481
BBIS104995754
CHX102177186
OAS100048991(KLK1)
BTAX128063377
ODA120872025(KLK1)
CCAD122421576(KLK1)
MBEZ129546491(KLK1)
SSC431673(KLK1)
CFR102515972(KLK1)
CBAI105062677
CDK105100157(KLK1)
VPC102528270(KLK1)
BACU103007165(KLK1)
BMUS118885121(KLK1) 118904290
LVE103081797(KLK1)
OOR101283477
DLE111181109(KLK1)
PCAD102980618
PSIU116743839
NASI112415494
ECB100034023(KLK1E2) 100147008(KLK1) 102147584 111775413
EAI106845317 106845494 123275590 123281043
MYB102251175(KLK1)
MYD102765308(KLK1)
MMYO118649263(KLK1)
EFUS103297602(KLK1)
MNA107531831(KLK1)
DRO112310143(KLK1)
AJM119052016(KLK1)
PDIC114511508(KLK1)
PHAS123830267(KLK1)
MMF118638349(KLK1)
PPAM129082971(KLK1)
HAI109390988(KLK1)
RFQ117016273 117019016 117035625(KLK1)
PALE102893946(KLK1) 102898477
PGIG120584017(KLK1)
PVP105307422(KLK1)
RAY107500469(KLK1)
MJV108397931(KLK1)
TOD119249652 119249656(KLK1)
SARA101548172 101548436 105942741
LAV104845473 111749208
TMU101344800
ETF101656202
DNM101416554 101430451 101437536 111766066
OAA100087855(KLK1)
CTIG120300122
CSAI133422322
XHE116718752
PRET103465468
PFOR107833457
PMEI106920573
GAF122830864 122846929
GFS119638812
AMER121594399
BCOO119068287
FAS105266686
AGRG126742270 126742273
CCRN123293478 123298016
DVT126897960
TPAL117649754
OSN115212877
 » show all
Reference
1  [PMID:7043199]
  Authors
Fiedler F, Fink E, Tschesche H, Fritz H.
  Title
Porcine glandular kallikreins.
  Journal
Methods Enzymol 80 Pt C:493-532 (1981)
DOI:10.1016/s0076-6879(81)80042-0
  Sequence
[ssc:431673]
Reference
2  [PMID:6295764]
  Authors
Anundi H, Ronne H, Peterson PA, Rask L.
  Title
Partial amino-acid sequence of the epidermal growth-factor-binding protein.
  Journal
Eur J Biochem 129:365-71 (1982)
DOI:10.1111/j.1432-1033.1982.tb07059.x
Reference
3  [PMID:6295383]
  Authors
Pesquero JL, Boschcov P, Oliveira MC, Paiva AC.
  Title
Effect of substrate size on tonin activity.
  Journal
Biochem Biophys Res Commun 108:1441-6 (1982)
DOI:10.1016/S0006-291X(82)80068-5
Reference
4  [PMID:6097352]
  Authors
Gutkowska J, Corvol P, Figueiredo AF, Inagami T, Bouhnik J, Genest J
  Title
Kinetic studies of rat renin and tonin on purified rat angiotensinogen.
  Journal
Can J Biochem Cell Biol 62:137-42 (1984)
DOI:10.1139/o84-020
Reference
5  [PMID:3844939]
  Authors
Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S.
  Title
Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins.
  Journal
Biochem Biophys Res Commun 127:289-95 (1985)
DOI:10.1016/S0006-291X(85)80157-1
Reference
6  [PMID:3691800]
  Authors
Akiyama K, Nakamura T, Iwanaga S, Hara M.
  Title
The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein.
  Journal
FEBS Lett 225:168-72 (1987)
DOI:10.1016/0014-5793(87)81151-1
Reference
7  [PMID:3036794]
  Authors
Evans BA, Drinkwater CC, Richards RI.
  Title
Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus.
  Journal
J Biol Chem 262:8027-34 (1987)
  Sequence
[mmu:16623]
Reference
8  [PMID:3643848]
  Authors
Fiedler F.
  Title
Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin.
  Journal
Eur J Biochem 163:303-12 (1987)
DOI:10.1111/j.1432-1033.1987.tb10801.x
Reference
9  [PMID:2821276]
  Authors
Fujinaga M, James MN.
  Title
Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution.
  Journal
J Mol Biol 195:373-96 (1987)
DOI:10.1016/0022-2836(87)90658-9
  Sequence
[rno:24841]
Reference
10 [PMID:3482210]
  Authors
Kato H, Nakanishi E, Enjyoji K, Hayashi I, Oh-ishi S, Iwanaga S
  Title
Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes.
  Journal
J Biochem 102:1389-404 (1987)
DOI:10.1093/oxfordjournals.jbchem.a122185
Reference
11 [PMID:3237072]
  Authors
Bailey GS.
  Title
Rat pancreas kallikrein.
  Journal
Methods Enzymol 163:115-28 (1988)
DOI:10.1016/0076-6879(88)63013-8
Reference
12 [PMID:2611215]
  Authors
Blaber M, Isackson PJ, Marsters JC Jr, Burnier JP, Bradshaw RA.
  Title
Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland.
  Journal
Biochemistry 28:7813-9 (1989)
DOI:10.1021/bi00445a043
Reference
13 [PMID:3070295]
  Authors
Chao J, Chao L.
  Title
Rat urinary kallikrein.
  Journal
Methods Enzymol 163:128-43 (1988)
DOI:10.1016/0076-6879(88)63014-x
Reference
14 [PMID:2975076]
  Authors
Zakrevskaia SF.
  Title
[Effectiveness of outpatient dental care for the schoolchildren of Arkhangelsk]
  Journal
Stomatologiia (Mosk) 67:62-3 (1988)
Reference
15 [PMID:2523317]
  Authors
Bertrand R, Derancourt J, Kassab R.
  Title
Selective cleavage at lysine of the 50 kDa-20 kDa connector loop segment of skeletal myosin S-1 by endoproteinase Arg-C.
  Journal
FEBS Lett 246:171-6 (1989)
DOI:10.1016/0014-5793(89)80277-7
Reference
16 [PMID:2708383]
  Authors
Wines DR, Brady JM, Pritchett DB, Roberts JL, MacDonald RJ.
  Title
Organization and expression of the rat kallikrein gene family.
  Journal
J Biol Chem 264:7653-62 (1989)
  Sequence
[rno:24594 24841]
Reference
17 [PMID:2194829]
  Authors
Elmoujahed A, Gutman N, Brillard M, Gauthier F.
  Title
Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland.
  Journal
FEBS Lett 265:137-40 (1990)
DOI:10.1016/0014-5793(90)80903-V
Reference
18 [PMID:2303430]
  Authors
Xiong W, Chen LM, Chao J.
  Title
Purification and characterization of a kallikrein-like T-kininogenase.
  Journal
J Biol Chem 265:2822-7 (1990)
  Sequence
[rno:292858]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.35
IUBMB Enzyme Nomenclature: 3.4.21.35
ExPASy - ENZYME nomenclature database: 3.4.21.35
BRENDA, the Enzyme Database: 3.4.21.35
CAS: 389069-73-2

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