DAPB1_PSEMX
ID DAPB1_PSEMX Reviewed; 723 AA.
AC O07834;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Dipeptidyl aminopeptidase BI {ECO:0000303|PubMed:9469937, ECO:0000312|EMBL:BAA20518.1};
DE Short=DAP BI {ECO:0000303|PubMed:8631703, ECO:0000303|PubMed:9469937};
DE EC=3.4.14.- {ECO:0000269|PubMed:8631703, ECO:0000269|PubMed:9469937};
DE Flags: Precursor;
GN Name=dapb1 {ECO:0000312|EMBL:BAA20518.1};
OS Pseudoxanthomonas mexicana.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=128785;
RN [1] {ECO:0000312|EMBL:BAA20518.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=WO24 {ECO:0000312|EMBL:BAA20518.1};
RX PubMed=9469937; DOI=10.1016/s0378-1119(97)00590-8;
RA Ogasawara W., Kobayashi G., Ishimaru S., Okada H., Morikawa Y.;
RT "The gene encoding dipeptidyl aminopeptidase BI from Pseudomonas sp. WO24:
RT cloning, sequencing and expression in Escherichia coli.";
RL Gene 206:229-236(1998).
RN [2]
RP PROTEIN SEQUENCE OF 24-41, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=WO24 {ECO:0000303|PubMed:8631703};
RX PubMed=8631703; DOI=10.1128/jb.178.5.1283-1288.1996;
RA Ogasawara W., Ochiai K., Ando K., Yano K., Yamasaki M., Okada H.,
RA Morikawa Y.;
RT "A novel dipeptidyl aminopeptidase from Pseudomonas sp. strain WO24.";
RL J. Bacteriol. 178:1283-1288(1996).
CC -!- FUNCTION: Sequentially removes dipeptide units (NH3-P2-P1-) from the
CC amino termini of peptides and proteins. Is able to catalyze the removal
CC of Asp-Arg from the amino termini of angiotensins I and II. Has slight
CC endopeptidase activity on N-terminally blocked peptide derivatives
CC which contain arginine residues at the P1 position. Does not hydrolyze
CC Ala-Ala-Ala and Ala-Ala-Ala-Ala substrates or isulin beta chain.
CC {ECO:0000269|PubMed:8631703}.
CC -!- ACTIVITY REGULATION: Nearly completely inhibited by 0.5 mM ZnCl(2), 0.1
CC mM N-tosyl-L-lysyl chloromethyl ketone (TLCK) and 0.1 mM leupeptin.
CC Strongly inhibited by 0.5 mM CoCl(2) and 0.1 mM chymostatin. Activity
CC is hardly affected by general serine protease inhibitors
CC phenylmethanesulfonyl fluoride (PMSF), diisopropyl fluorophosphate
CC (DFP) and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK) or by
CC aspartyl protease inhibitor pepstatin A or by CaCl(2) and EDTA.
CC Cysteine protease inhibitors, such as N-ethylmaleimide (NEM),
CC iodoacetic acid and L-trans-epoxysuccinyl-leucylamido(4-guanido)butane
CC (E-64) have no effect on activity. {ECO:0000269|PubMed:8631703,
CC ECO:0000269|PubMed:9469937}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for Gly-Arg-pNA (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8631703};
CC KM=0.019 mM for Arg-Arg-4-methoxy-beta-naphthylamide (Arg-Arg-MNA)
CC (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703};
CC KM=0.052 mM for Gly-Arg-MNA (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8631703};
CC Vmax=195 umol/min/mg enzyme with Gly-Arg-pNA as substrate (at pH 9
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8631703};
CC Vmax=145 umol/min/mg enzyme with Arg-Arg-MNA as substrate (at pH 9
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8631703};
CC Vmax=95 umol/min/mg enzyme with Gly-Arg-MNA as substrate (at pH 9 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:8631703};
CC pH dependence:
CC Optimum pH is 9.0 for the hydrolysis of Gly-Arg-pNA. No hydrolysis of
CC Gly-Arg-pNA is detected below pH 5.5 or above pH 11.5. Stable over a
CC broad pH range of between 7.5 and 10.0. {ECO:0000269|PubMed:8631703};
CC Temperature dependence:
CC Optimum temperature is between 35 and 40 degrees Celsius for the
CC hydrolysis of Gly-Arg-pNA. Stable for at least 30 minutes below 20
CC degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8631703}.
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; AB004795; BAA20518.1; -; Genomic_DNA.
DR AlphaFoldDB; O07834; -.
DR SMR; O07834; -.
DR ESTHER; psesp-DAP; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.010; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Protease;
KW Serine protease; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8631703"
FT CHAIN 24..723
FT /note="Dipeptidyl aminopeptidase BI"
FT /id="PRO_0000433467"
FT ACT_SITE 574
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P24555,
FT ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 659
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 694
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ SEQUENCE 723 AA; 80754 MW; D480FBC28FD78BC7 CRC64;
MKPTSLLLAA TVLMSTPITS ALAASATPPD VAKKPHVVKA PHGAERNDEY YWLRDDKREN
KEMLAYLNAE NAYTDAVMAP LKPLEDKLYD EVVARIKQDD ASVPYRERGW WYYARFVTGK
DYPVHARRKD GPGVDAVSIQ AANAAGDFAG EQVLLDVNAL GAGKDYYNVG DYEVSQDNRL
LAYADDTNGR RQYTIRFKNL DTGELLPDTV TNAEPNLVWS DDGRTLFYVD KDPETLLSKR
VKAHVLGTPA SQDALVYEEE DDSFYMGIGR SRDDKFICIS VESTVSSEMR CTPAASPGVF
TVLAPRERDV EYQADHLGDR WVIRTNADGA TNFKIVTAPT DSTSRKDWKD WVAHRDDVFV
EGFELFDGFS VVAERANALE SLRVIKADGS SDYVKADESA YSMGLSANPE TGTDWLRYSY
TSMTTPATTY EINTKTGERR QLKQQPVPGY DASKYVTERV WAPARDGKTK IPVTLVYRKD
VARDGKAPML QYAYGSYGAS MDPNFSITNV SLLDRGVVYA LAHIRGGQEM GRAWYDDGKL
YNKINTFTDF IDVTDYLVKE GYAAKDRVAA MGGSAGGLLM GAVSNMAPEK YKVILTLVPF
VDVVTTMLDP TIPLTTNEYD EWGNPEEKGY YDYILTYSPY DNLQAKAYPA MFVGTGLWDS
QVQYWEPAKY VARLRDLNTG KGPVVFRTNM EAGHGGKSGR FRQYRERAEM FAFMLDQLGV
ASK
