AAM_RHOER
ID AAM_RHOER Reviewed; 477 AA.
AC K9NBS6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Acylamidase {ECO:0000303|PubMed:21073421};
DE EC=3.5.1.13 {ECO:0000269|PubMed:21073421};
DE EC=3.5.1.14 {ECO:0000269|PubMed:21073421};
DE EC=3.5.1.4 {ECO:0000269|PubMed:21073421};
GN Name=aam {ECO:0000303|Ref.1};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=TA37;
RX DOI=10.1134/S1022795413070090;
RA Lavrov K.V., Yanenko A.S.;
RT "Cloning of new acylamidase gene from Rhodococcus erythropolis and its
RT expression in Escherichia coli.";
RL Russ. J. Genet. 49:1078-1081(2013).
RN [2]
RP PROTEIN SEQUENCE OF 2-13; 125-136 AND 455-466, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=TA37;
RX PubMed=21073421; DOI=10.1134/s0006297910080080;
RA Lavrov K.V., Zalunin I.A., Kotlova E.K., Yanenko A.S.;
RT "A new acylamidase from Rhodococcus erythropolis TA37 can hydrolyze N-
RT substituted amides.";
RL Biochemistry (Mosc.) 75:1006-1013(2010).
CC -!- FUNCTION: Amidase with broad substrate specificity, catalyzing the
CC hydrolysis of a wide range of N-substituted amides, and, to a lesser
CC extent, the hydrolysis of non-substituted amides. Acid para-
CC nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the
CC best substrates for this enzyme. N-substituted acrylamides (isopropyl
CC acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-
CC acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and
CC aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide,
CC and valeramide) can also be used as substrates but with less
CC efficiency. {ECO:0000269|PubMed:21073421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000269|PubMed:21073421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an anilide + H2O = a carboxylate + aniline + H(+);
CC Xref=Rhea:RHEA:20297, ChEBI:CHEBI:13248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17296, ChEBI:CHEBI:29067; EC=3.5.1.13;
CC Evidence={ECO:0000269|PubMed:21073421, ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
CC Evidence={ECO:0000269|PubMed:21073421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-
CC substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718; EC=3.5.1.14;
CC -!- ACTIVITY REGULATION: Amidase activity is completely suppressed by
CC inhibitors of serine proteases (phenylmethylsulfonyl fluoride and
CC diisopropyl fluorophosphate), partially inhibited by copper and mercury
CC ions, but is not affected by inhibitors of aliphatic amidases
CC (acetaldehyde and nitrophenyl disulfides) or by EDTA.
CC {ECO:0000269|PubMed:21073421}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for Gly-para-nitroanilide {ECO:0000269|PubMed:21073421};
CC KM=0.48 mM for Leu-para-nitroanilide {ECO:0000269|PubMed:21073421};
CC KM=0.55 mM for Ala-para-nitroanilide {ECO:0000269|PubMed:21073421};
CC Vmax=104.5 umol/min/mg enzyme with Gly-para-nitroanilide as substrate
CC {ECO:0000269|PubMed:21073421};
CC Vmax=17.0 umol/min/mg enzyme with Leu-para-nitroanilide as substrate
CC {ECO:0000269|PubMed:21073421};
CC Vmax=35.5 umol/min/mg enzyme with Ala-para-nitroanilide as substrate
CC {ECO:0000269|PubMed:21073421};
CC pH dependence:
CC Optimum pH is 7-8. At low pH values the enzyme is rapidly
CC inactivated, whereas in basic medium inactivation is rather slow.
CC {ECO:0000269|PubMed:21073421};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Shows a drastic decrease
CC in activity above the optimal temperature. Is stable for 15 hours at
CC 22 degrees Celsius and for 0.5 hour at 45 degrees Celsius.
CC {ECO:0000269|PubMed:21073421};
CC -!- INDUCTION: By acetanilide. {ECO:0000269|PubMed:21073421}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; JX894244; AFY17041.1; -; Genomic_DNA.
DR AlphaFoldDB; K9NBS6; -.
DR SMR; K9NBS6; -.
DR STRING; 1833.XU06_20045; -.
DR GO; GO:0004040; F:amidase activity; IDA:UniProtKB.
DR GO; GO:0004046; F:aminoacylase activity; IDA:UniProtKB.
DR GO; GO:0047680; F:aryl-acylamidase activity; IDA:UniProtKB.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0043605; P:cellular amide catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:21073421"
FT CHAIN 2..477
FT /note="Acylamidase"
FT /id="PRO_0000424899"
FT ACT_SITE 82
FT /note="Charge relay system"
FT /evidence="ECO:0000305|Ref.1"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000305|Ref.1"
FT ACT_SITE 181
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305|Ref.1"
SQ SEQUENCE 477 AA; 51076 MW; 4CDE4F71C0905941 CRC64;
MTEQNLHWLS ATEMAASVAS NNLSPNEIAE AMIQRVDAVN PSINAIVQFD REQVTRDAAE
LSRQQEAGEK LGPLHGVPFT IKDLTAVDGL PTTFGMKPMA DNIATGNAVV VDRLRGAGGL
FLGKTNTPES GYYGGTDNHL YGPTHNPWKL GNSAGGSSGG ASAAVAAGLG PLAEGSDGAG
SVRIPSALCG VVGLKPTTGV IPQTILAGRF YNWAYHGPIT RTVADNALML DIMAGPDNAD
PLSIERAETS YVEASKGDVK GLRVAWSPNL GLGHVDPEVL AVCLDALAAF EELGAQITEA
TPQWGNPSES MWSGIWVPGF ASEYDLLDWE NQRGEVDDYL IEIMHEAERL TGVDVGRADA
FRGDMWDTWT TFMNDYDVLV SPTLASATFP LRQFAPSWLE GASLREQLLD WLFTYPYNML
NNPAITVPAG FTADGRPVGL QIAARHRRDA LVLRTAANFE AVRPWADKKP ADSLVVA
