DHDH_MACFU
ID DHDH_MACFU Reviewed; 334 AA.
AC Q7JK39;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
DE EC=1.3.1.20;
DE AltName: Full=D-xylose 1-dehydrogenase;
DE AltName: Full=D-xylose-NADP dehydrogenase;
DE EC=1.1.1.179;
DE AltName: Full=Dimeric dihydrodiol dehydrogenase;
DE AltName: Full=Jmo2DD;
GN Name=DHDH; Synonyms=2DD;
OS Macaca fuscata fuscata (Japanese macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9543;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-80; 92-97; 99-105;
RP 137-148; 174-180; 245-262; 267-290 AND 302-333, SUBUNIT, TISSUE
RP SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney;
RX PubMed=10477285; DOI=10.1042/bj3420721;
RA Arimitsu E., Aoki S., Ishikura S., Nakanishi K., Matsuura K., Hara A.;
RT "Cloning and sequencing of the cDNA species for mammalian dimeric
RT dihydrodiol dehydrogenases.";
RL Biochem. J. 342:721-728(1999).
RN [2]
RP SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-79 AND TYR-180.
RX PubMed=11097839; DOI=10.1006/bbrc.2000.3796;
RA Asada Y., Aoki S., Ishikura S., Usami N., Hara A.;
RT "Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in
RT catalytic function.";
RL Biochem. Biophys. Res. Commun. 278:333-337(2000).
RN [3]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Kidney;
RX PubMed=11306093; DOI=10.1016/s0009-2797(00)00307-0;
RA Aoki S., Ishikura S., Asada Y., Usami N., Hara A.;
RT "Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-
RT xylose dehydrogenase in pig liver.";
RL Chem. Biol. Interact. 130:775-784(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol +
CC H(+) + NADPH; Xref=Rhea:RHEA:16729, ChEBI:CHEBI:10702,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.20;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.179;
CC -!- ACTIVITY REGULATION: Strongly inhibited by isoascorbic acid, 4-
CC hydroxyacetophenone and chloromercuriphenylsulphonate. Stimulated by
CC various salts. {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11097839, ECO:0000269|PubMed:11306093}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for naphthalene dihydrodiol (at pH 10.0)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC KM=0.9 mM for benzene dihydrodiol (at pH 10.0)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC KM=1.2 mM for 3-deoxyglucosone (at pH 7.5)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC KM=0.12 mM for camphorquinone (at pH 7.5)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC KM=1.3 mM for methylglyoxal (at pH 7.5) {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11306093};
CC KM=6.4 mM for D-xylose (at pH 7.5) {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11306093};
CC KM=29 mM for D-glucose (at pH 7.5) {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11306093};
CC Vmax=36 umol/min/mg enzyme with naphthalene dihydrodiol as substrate
CC (at pH 10.0) {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11306093};
CC Vmax=16 umol/min/mg enzyme with benzene dihydrodiol as substrate (at
CC pH 10.0) {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC Vmax=17 umol/min/mg enzyme with reduced 3-deoxyglucosone as substrate
CC (at pH 7.5) {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11306093};
CC Vmax=34 umol/min/mg enzyme with camphorquinone as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC Vmax=10 umol/min/mg enzyme with methylglyoxal as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC Vmax=9.0 umol/min/mg enzyme with D-xylose as substrate (at pH 7.5)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC Vmax=1.1 umol/min/mg enzyme with D-glucose as substrate (at pH 7.5)
CC {ECO:0000269|PubMed:10477285, ECO:0000269|PubMed:11306093};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10477285,
CC ECO:0000269|PubMed:11097839}.
CC -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:10477285}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AB021931; BAA83488.1; -; mRNA.
DR AlphaFoldDB; Q7JK39; -.
DR SMR; Q7JK39; -.
DR SABIO-RK; Q7JK39; -.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..334
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315363"
FT SITE 71
FT /note="May play an important role in coenzyme binding"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="May play an important role in coenzyme binding"
FT SITE 97
FT /note="May play an important role in coenzyme binding"
FT /evidence="ECO:0000250"
FT SITE 176
FT /note="May play an important role for the adaptation of the
FT alcohol substrate into the binding site"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="May play an important role in catalytic activity"
FT MUTAGEN 79
FT /note="H->E: Decrease in K(d) and K(m) value for NADPH.
FT Elimination of the fluorescence-energy transfer and
FT enhancement of NADPH fluorescence by the binary complex
FT formation. Potent inhibition of the dehydrogenase activity
FT by high ionic strength."
FT /evidence="ECO:0000269|PubMed:11097839"
FT MUTAGEN 180
FT /note="Y->F: Significant loss of activity. No effect on the
FT high affinity for NADPH, fluorescence-energy transfer and
FT enhancement of NADPH fluorescence by the binary complex
FT formation."
FT /evidence="ECO:0000269|PubMed:11097839"
SQ SEQUENCE 334 AA; 36435 MW; D319AF45660667C9 CRC64;
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE
LAKDPNVEVA YVGTQHPQHK AAVMLCLAAG KAVLCEKPMG VNAAEVREMV TEARSRGLFL
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLTH VPRAVDWAQA GGALLDLGIY
CVQFISMVFG GQKPEKISVM GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV
SGTKGMAQLL NPCWCPTELV VKGEHKEFLL PPVPKNCNFD NGAGMSYEAK HVRECLRKGL
KESPVIPLVE SELLADILEE VRRAIGVTFP QDKH
