AGAA_CORST
ID AGAA_CORST Reviewed; 400 AA.
AC Q8GGD4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=N(alpha)-acyl-glutamine aminoacylase {ECO:0000303|PubMed:17193210};
DE Short=N-AGA {ECO:0000303|PubMed:17193210};
DE EC=3.5.1.133 {ECO:0000269|PubMed:12468539, ECO:0000269|PubMed:17193210, ECO:0000269|PubMed:18492161};
DE AltName: Full=Axillary malodor releasing enzyme {ECO:0000303|PubMed:18492161};
DE Short=AMRE {ECO:0000303|PubMed:18492161};
GN Name=agaA {ECO:0000303|PubMed:12468539};
OS Corynebacterium striatum.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=43770;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-37, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=Ax20;
RX PubMed=12468539; DOI=10.1074/jbc.m210142200;
RA Natsch A., Gfeller H., Gygax P., Schmid J., Acuna G.;
RT "A specific bacterial aminoacylase cleaves odorant precursors secreted in
RT the human axilla.";
RL J. Biol. Chem. 278:5718-5727(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOTECHNOLOGY.
RC STRAIN=Ax20;
RX PubMed=18492161; DOI=10.1111/j.1467-2494.2004.00255.x;
RA Natsch A., Gfeller H., Gygax P., Schmid J.;
RT "Isolation of a bacterial enzyme releasing axillary malodor and its use as
RT a screening target for novel deodorant formulations.";
RL Int. J. Cosmet. Sci. 27:115-122(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Ax20;
RX PubMed=17193210; DOI=10.1002/cbdv.200690015;
RA Natsch A., Derrer S., Flachsmann F., Schmid J.;
RT "A broad diversity of volatile carboxylic acids, released by a bacterial
RT aminoacylase from axilla secretions, as candidate molecules for the
RT determination of human-body odor type.";
RL Chem. Biodivers. 3:1-20(2006).
CC -!- FUNCTION: Hydrolyzes odorless N-alpha-acyl-L-glutamine conjugates of
CC short- and medium-chain fatty acids, releasing human axillary malodor
CC compounds (PubMed:12468539, PubMed:18492161, PubMed:17193210). The
CC enzyme is highly specific for the glutamine residue but has a low
CC specificity for the acyl part of the substrate (PubMed:12468539,
CC PubMed:18492161, PubMed:17193210). The two most common products are 3-
CC methyl-2-hexenoic acid (3M2H) and 3-hydroxy-3-methyl-hexanoic acid
CC (HMHA), which are produced from the odorless precursors N-alpha-3-
CC methyl-2-hexenoyl-L-glutamine (3M2H-Gln) and N-alpha-3-hydroxy-3-
CC methylhexanoyl-L-glutamine (HMHA-Gln) (PubMed:12468539,
CC PubMed:18492161, PubMed:17193210). In addition, over 28 different
CC carboxylic acids contributing to human body odor are released by this
CC enzyme from odorless axilla secretions, including several aliphatic 3-
CC hydroxy acids with 4-Me branches, 3,4-unsaturated, 4-Et-branched
CC aliphatic acids, and a variety of degradation products of amino acids
CC (PubMed:17193210). {ECO:0000269|PubMed:12468539,
CC ECO:0000269|PubMed:17193210, ECO:0000269|PubMed:18492161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-acyl-L-glutamine + H2O = a carboxylate + L-glutamine;
CC Xref=Rhea:RHEA:59984, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:87584; EC=3.5.1.133;
CC Evidence={ECO:0000269|PubMed:12468539, ECO:0000269|PubMed:17193210,
CC ECO:0000269|PubMed:18492161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-[(2E)-3-methylhex-2-enoyl]-L-glutaminate = (2E)-3-
CC methylhex-2-enoate + L-glutamine; Xref=Rhea:RHEA:60040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58359, ChEBI:CHEBI:143557,
CC ChEBI:CHEBI:143558; EC=3.5.1.133;
CC Evidence={ECO:0000269|PubMed:12468539, ECO:0000269|PubMed:17193210,
CC ECO:0000269|PubMed:18492161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(3-hydroxy-3-methylhexanoyl)-L-glutaminate = 3-
CC hydroxy-3-methylhexanoate + L-glutamine; Xref=Rhea:RHEA:60036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58359, ChEBI:CHEBI:143555,
CC ChEBI:CHEBI:143556; EC=3.5.1.133;
CC Evidence={ECO:0000269|PubMed:12468539, ECO:0000269|PubMed:17193210,
CC ECO:0000269|PubMed:18492161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12468539, ECO:0000269|PubMed:17193210,
CC ECO:0000269|PubMed:18492161};
CC -!- ACTIVITY REGULATION: Partial loss of activity with the combination
CC Mn(2+) and chelating agents. Activity is lost in presence of 0.5 mM
CC dithiothreitol. {ECO:0000269|PubMed:12468539}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for 3M2H-Gln {ECO:0000269|PubMed:12468539};
CC KM=0.74 mM for HMHA-Gln {ECO:0000269|PubMed:12468539};
CC KM=0.08 mM for N-alpha-decanoyl-L-glutamine
CC {ECO:0000269|PubMed:12468539};
CC KM=0.06 mM for N-alpha-lauroyl-L-glutamine
CC {ECO:0000269|PubMed:12468539};
CC KM=0.05 mM for carbobenzyloxy-L-glutamine
CC {ECO:0000269|PubMed:12468539};
CC KM=0.115 mM for N2-[(3E)-4-methyloct-3-enoyl]-L-glutamine
CC {ECO:0000269|PubMed:17193210};
CC KM=0.25 mM for N2-[(3S)-3-hydroxy-4-methylheptanoyl]glutamine
CC {ECO:0000269|PubMed:17193210};
CC Vmax=0.121 mmol/min/mg enzyme with 3M2H-Gln as substrate
CC {ECO:0000269|PubMed:12468539};
CC Vmax=0.461 mmol/min/mg enzyme with HMHA-Gln as substrate
CC {ECO:0000269|PubMed:12468539};
CC Vmax=0.752 mmol/min/mg enzyme with N-alpha-decanoyl-L-glutamine as
CC substrate {ECO:0000269|PubMed:12468539};
CC Vmax=0.325 mmol/min/mg enzyme with N-alpha-lauroyl-L-glutamine as
CC substrate {ECO:0000269|PubMed:12468539};
CC Vmax=0.065 mmol/min/mg enzyme with carbobenzyloxy-L-glutamine as
CC substrate {ECO:0000269|PubMed:12468539};
CC Vmax=0.83 mmol/min/mg enzyme with N2-[(3E)-4-methyloct-3-enoyl]-L-
CC glutamine as substrate {ECO:0000269|PubMed:17193210};
CC Vmax=0.51 mmol/min/mg enzyme with N2-[(3S)-3-hydroxy-4-
CC methylheptanoyl]glutamine as substrate {ECO:0000269|PubMed:17193210};
CC -!- BIOTECHNOLOGY: The elucidation of the enzymatic mechanisms of malodor
CC formation may lead to completely new ways to design deodorant actives.
CC A targeted approach to block the enzymatic process offers the
CC possibility of an efficient treatment without perturbation of the
CC resident skin microflora. The enzyme could also be fed with alternative
CC substrates which are designed to release a fragrance note instead of
CC the malodor. {ECO:0000269|PubMed:18492161}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; AF534871; AAN77164.1; -; Genomic_DNA.
DR PDB; 6SLF; X-ray; 1.75 A; A/B/C/D=1-400.
DR PDBsum; 6SLF; -.
DR AlphaFoldDB; Q8GGD4; -.
DR SMR; Q8GGD4; -.
DR KEGG; ag:AAN77164; -.
DR BioCyc; MetaCyc:MON-20502; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR11014; PTHR11014; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01891; amidohydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12468539"
FT CHAIN 2..400
FT /note="N(alpha)-acyl-glutamine aminoacylase"
FT /id="PRO_0000450523"
FT HELIX 4..29
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6SLF"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 256..268
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 269..289
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 311..325
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:6SLF"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6SLF"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:6SLF"
SQ SEQUENCE 400 AA; 43494 MW; ABCD0E806DE1030E CRC64;
MAQENLQKIV DSLESSRAER EELYKWFHQH PEMSMQEHET SKRIAEELEK LGLEPQNIGV
TGQVAVIKNG EGPSVAFRAD FDALPITENT GLDYSADPEL GMMHACGHDL HTTALLGAVR
ALVENKDLWS GTFIAVHQPG EEGGGGARHM VDDGLAEKIA APDVCFAQHV FNEDPAFGYV
FTPGRFLTAA SNWRIHIHGE GGHGSRPHLT KDPIVVAASI ITKLQTIVSR EVDPNEVAVV
TVGSIEGGKS TNSIPYTVTL GVNTRASNDE LSEYVQNAIK RIVIAECQAA GIEQEPEFEY
LDSVPAVIND EDLTEQLMAQ FREFFGEDQA VEIPPLSGSE DYPFIPNAWG VPSVMWGWSG
FAAGSDAPGN HTDKFAPELP DALERGTQAI LVAAAPWLMK
