AKR_SYNY3
ID AKR_SYNY3 Reviewed; 327 AA.
AC P74308;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Aldo/keto reductase slr0942 {ECO:0000303|PubMed:24317062, ECO:0000303|PubMed:25376835};
DE Short=AKR {ECO:0000303|PubMed:24317062, ECO:0000303|PubMed:25376835};
DE EC=1.1.1.184 {ECO:0000269|PubMed:24317062, ECO:0000269|PubMed:25376835};
DE AltName: Full=AKR3G1 {ECO:0000303|PubMed:25376835};
GN OrderedLocusNames=slr0942 {ECO:0000312|EMBL:BAA18402.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=24317062; DOI=10.1271/bbb.130554;
RA Shimakawa G., Suzuki M., Yamamoto E., Nishi A., Saito R., Sakamoto K.,
RA Yamamoto H., Makino A., Miyake C.;
RT "Scavenging systems for reactive carbonyls in the cyanobacterium
RT Synechocystis sp. PCC 6803.";
RL Biosci. Biotechnol. Biochem. 77:2441-2448(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=25376835; DOI=10.1096/fj.14-258327;
RA Hintzpeter J., Martin H.J., Maser E.;
RT "Reduction of lipid peroxidation products and advanced glycation end-
RT product precursors by cyanobacterial aldo-keto reductase AKR3G1-a founding
RT member of the AKR3G subfamily.";
RL FASEB J. 29:263-273(2015).
CC -!- FUNCTION: Aldo/keto reductase with broad substrate spectrum. Catalyzes
CC the NADPH-dependent reduction of aldehyde- and ketone-groups of
CC different classes of carbonyl compounds to the corresponding alcohols.
CC Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE)
CC and 4-hydroxynon-2-enal (4-HNE), that are lipid peroxidation products,
CC and 9,10-phenanthrenequinone (9,10-PQ), a photoproduct of phenanthrene
CC that is one of the most prevalent polycyclic aromatic hydrocarbons in
CC the environment. Is also active on sugar-derived reactive carbonyls
CC such as methylglyoxal (MG), glyoxal and 3-deoxyglucosone (3-DG), and on
CC other lipid-derived carbonyls such as acrolein. May be involved in the
CC detoxification of the toxic lipid peroxidation products 4-ONE and 4-HNE
CC besides many other exo- and endogenic reactive carbonyl compounds (RCs)
CC that may lead to photoinhibition or other cell damages.
CC {ECO:0000269|PubMed:24317062, ECO:0000269|PubMed:25376835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH;
CC Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.184; Evidence={ECO:0000269|PubMed:24317062,
CC ECO:0000269|PubMed:25376835};
CC -!- ACTIVITY REGULATION: Curcumin non-competitively inhibits the enzyme
CC with respect to furfural. To a lesser extent, enzyme activity is also
CC inhibited by indomethacin, coumarate, coumarin, and alrestatin.
CC {ECO:0000269|PubMed:25376835}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for methylglyoxal {ECO:0000269|PubMed:24317062};
CC KM=10.8 mM for glyoxal {ECO:0000269|PubMed:24317062};
CC KM=520 uM for 3-deoxyglucosone {ECO:0000269|PubMed:24317062};
CC KM=1.7 mM for acrolein {ECO:0000269|PubMed:24317062};
CC KM=94 uM for hexanal {ECO:0000269|PubMed:25376835};
CC KM=94 uM for 4-pyridinecarboxaldehyde {ECO:0000269|PubMed:25376835};
CC KM=46 uM for 4-nitrobenzaldehyde {ECO:0000269|PubMed:25376835};
CC KM=5 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:25376835};
CC KM=4.7 uM for 4-oxonon-2-enal {ECO:0000269|PubMed:25376835};
CC KM=59.5 uM for 4-hydroxynon-2-enal {ECO:0000269|PubMed:25376835};
CC KM=890 uM for furfural {ECO:0000269|PubMed:25376835};
CC KM=8.5 uM for NADPH {ECO:0000269|PubMed:25376835};
CC Note=kcat is 351 min(-1) with methylglyoxal as substrate. kcat is
CC 1049 min(-1) with glyoxal as substrate. kcat is 226 min(-1) with 3-
CC deoxyglucosone as substrate. kcat is 1078 min(-1) with acrolein as
CC substrate. kcat is 1.75 sec(-1) with hexanal as substrate. kcat is
CC 1.17 sec(-1) with 4-pyridinecarboxaldehyde as substrate. kcat is 0.3
CC sec(-1) with 4-nitrobenzaldehyde as substrate. kcat is 2.23 sec(-1)
CC with 9,10-phenanthrenequinone as substrate. kcat is 4.06 sec(-1) with
CC 2,3-pentanedione as substrate. kcat is 2.63 sec(-1) with 4-oxonon-2-
CC enal as substrate. kcat is 1.57 sec(-1) with 4-hydroxynon-2-enal as
CC substrate. kcat is 8.52 sec(-1) with furfural as substrate.
CC {ECO:0000269|PubMed:24317062, ECO:0000269|PubMed:25376835};
CC pH dependence:
CC Optimum pH is 5 for the reduction of methylglyoxal.
CC {ECO:0000269|PubMed:24317062};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius for the reduction of
CC methylglyoxal. {ECO:0000269|PubMed:24317062};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25376835}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18402.1; -; Genomic_DNA.
DR PIR; S76143; S76143.
DR AlphaFoldDB; P74308; -.
DR SMR; P74308; -.
DR IntAct; P74308; 10.
DR STRING; 1148.1653489; -.
DR PaxDb; P74308; -.
DR EnsemblBacteria; BAA18402; BAA18402; BAA18402.
DR KEGG; syn:slr0942; -.
DR eggNOG; COG0656; Bacteria.
DR InParanoid; P74308; -.
DR OMA; AEMYANE; -.
DR PhylomeDB; P74308; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR CDD; cd19123; AKR_AKR3G1; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044496; AKR3G.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..327
FT /note="Aldo/keto reductase slr0942"
FT /id="PRO_0000431728"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT BINDING 18..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT BINDING 216..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT SITE 86
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P15121"
SQ SEQUENCE 327 AA; 36014 MW; 4B9415E098A8892D CRC64;
MQSFNRINSM KYFPLSNGEQ IPALGLGTWK SSPQVVGQAV EQALDLGYRH LDCAAIYGNE
AEIGATLANA FTKGVVKREE LWITSKLWSN AHHPDAVLPA LEKTLQDLGL DYLDLYLIHW
PVVIQPDVGF PESGDQLLPF TPASLEGTWQ ALEKAVDLGL CHHIGVSNFS LKKLEMVLSM
ARIPPAVNQV ELHPYLQQSD LLTFANSQNI LLTAYSPLGS GDRPAAFQQA AEPKLLTDPV
INGIAAEQGC SAAQVLLAWA IQRGTVTIPK SVNPERLEQN LRAADITLTD SEMAKIALLD
RHYRYVSGDF WTMPGSPYTL QNLWDEI
