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Acylamidase (EC 3.5.1.13) (EC 3.5.1.14) (EC 3.5.1.4)

 AAM_RHOER               Reviewed;         477 AA.
K9NBS6;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
05-JUL-2017, entry version 12.
RecName: Full=Acylamidase;
EC=3.5.1.13;
EC=3.5.1.14;
EC=3.5.1.4;
Name=aam;
Rhodococcus erythropolis (Arthrobacter picolinophilus).
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
Rhodococcus.
NCBI_TaxID=1833;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
STRAIN=TA37;
DOI=10.1134/S1022795413070090;
Lavrov K.V., Yanenko A.S.;
"Cloning of new acylamidase gene from Rhodococcus erythropolis and its
expression in Escherichia coli.";
Russ. J. Genet. 49:1078-1081(2013).
[2]
PROTEIN SEQUENCE OF 2-13; 125-136 AND 455-466, FUNCTION, CATALYTIC
ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND INDUCTION.
STRAIN=TA37;
PubMed=21073421; DOI=10.1134/S0006297910080080;
Lavrov K.V., Zalunin I.A., Kotlova E.K., Yanenko A.S.;
"A new acylamidase from Rhodococcus erythropolis TA37 can hydrolyze N-
substituted amides.";
Biochemistry (Mosc.) 75:1006-1013(2010).
-!- FUNCTION: Amidase with broad substrate specificity, catalyzing the
hydrolysis of a wide range of N-substituted amides, and, to a
lesser extent, the hydrolysis of non-substituted amides. Acid
para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-
pNA) are the best substrates for this enzyme. N-substituted
acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl
acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of
glycine, alanine and leucine, and aliphatic amides (acetamide,
acrylamide, isobutyramide, n-butyramide, and valeramide) can also
be used as substrates but with less efficiency.
{ECO:0000269|PubMed:21073421}.
-!- CATALYTIC ACTIVITY: A monocarboxylic acid amide + H(2)O = a
monocarboxylate + NH(3).
-!- CATALYTIC ACTIVITY: An anilide + H(2)O = a carboxylate + aniline.
-!- CATALYTIC ACTIVITY: An N-acyl-aliphatic-L-amino acid + H(2)O = an
aliphatic L-amino acid + a carboxylate.
-!- CATALYTIC ACTIVITY: An N-acetyl-L-cysteine-S-conjugate + H(2)O =
an L-cysteine-S-conjugate + acetate.
-!- ENZYME REGULATION: Amidase activity is completely suppressed by
inhibitors of serine proteases (phenylmethylsulfonyl fluoride and
diisopropyl fluorophosphate), partially inhibited by copper and
mercury ions, but is not affected by inhibitors of aliphatic
amidases (acetaldehyde and nitrophenyl disulfides) or by EDTA.
{ECO:0000269|PubMed:21073421}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.25 mM for Gly-para-nitroanilide
{ECO:0000269|PubMed:21073421};
KM=0.48 mM for Leu-para-nitroanilide
{ECO:0000269|PubMed:21073421};
KM=0.55 mM for ALa-para-nitroanilide
{ECO:0000269|PubMed:21073421};
Vmax=104.5 umol/min/mg enzyme with Gly-para-nitroanilide as
substrate {ECO:0000269|PubMed:21073421};
Vmax=17.0 umol/min/mg enzyme with Leu-para-nitroanilide as
substrate {ECO:0000269|PubMed:21073421};
Vmax=35.5 umol/min/mg enzyme with Ala-para-nitroanilide as
substrate {ECO:0000269|PubMed:21073421};
pH dependence:
Optimum pH is 7-8. At low pH values the enzyme is rapidly
inactivated, whereas in basic medium inactivation is rather
slow. {ECO:0000269|PubMed:21073421};
Temperature dependence:
Optimum temperature is 55 degrees Celsius. Shows a drastic
decrease in activity above the optimal temperature. Is stable
for 15 hours at 22 degrees Celsius and for 0.5 hour at 45
degrees Celsius. {ECO:0000269|PubMed:21073421};
-!- INDUCTION: By acetanilide. {ECO:0000269|PubMed:21073421}.
-!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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EMBL; JX894244; AFY17041.1; -; Genomic_DNA.
SMR; K9NBS6; -.
eggNOG; ENOG4105DV0; Bacteria.
eggNOG; COG0154; LUCA.
GO; GO:0004040; F:amidase activity; IDA:UniProtKB.
GO; GO:0004046; F:aminoacylase activity; IDA:UniProtKB.
GO; GO:0047680; F:aryl-acylamidase activity; IDA:UniProtKB.
GO; GO:0043605; P:cellular amide catabolic process; IDA:UniProtKB.
Gene3D; 3.90.1300.10; -; 1.
InterPro; IPR000120; Amidase.
InterPro; IPR020556; Amidase_CS.
InterPro; IPR023631; Amidase_dom.
PANTHER; PTHR11895; PTHR11895; 1.
Pfam; PF01425; Amidase; 1.
SUPFAM; SSF75304; SSF75304; 1.
PROSITE; PS00571; AMIDASES; 1.
1: Evidence at protein level;
Direct protein sequencing; Hydrolase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:21073421}.
CHAIN 2 477 Acylamidase.
/FTId=PRO_0000424899.
ACT_SITE 82 82 Charge relay system. {ECO:0000250}.
ACT_SITE 157 157 Charge relay system. {ECO:0000250}.
ACT_SITE 181 181 Acyl-ester intermediate. {ECO:0000250}.
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


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