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[1]
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NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-80; 92-97; 99-105; 137-148; 174-180; 245-262; 267-290 AND 302-333, SUBUNIT, TISSUE SPECIFICITY, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Kidney;
DOI=10.1042/0264-6021:3420721; PubMed=10477285 [NCBI, ExPASy, EBI, Israel, Japan]
Arimitsu E.,
Aoki S.,
Ishikura S.,
Nakanishi K.,
Matsuura K.,
Hara A.;
"Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases.";
Biochem. J. 342:721-728(1999).
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[2]
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SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF HIS-79 AND TYR-180.
DOI=10.1006/bbrc.2000.3796; PubMed=11097839 [NCBI, ExPASy, EBI, Israel, Japan]
Asada Y.,
Aoki S.,
Ishikura S.,
Usami N.,
Hara A.;
"Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function.";
Biochem. Biophys. Res. Commun. 278:333-337(2000).
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[3]
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ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Kidney;
DOI=10.1016/S0009-2797(00)00307-0; PubMed=11306093 [NCBI, ExPASy, EBI, Israel, Japan]
Aoki S.,
Ishikura S.,
Asada Y.,
Usami N.,
Hara A.;
"Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-xylose dehydrogenase in pig liver.";
Chem. Biol. Interact. 130:775-784(2001).
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- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
- CATALYTIC ACTIVITY: D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH.
- ENZYME REGULATION: Strongly inhibited by isoascorbic acid, 4-hydroxyacetophenone and chloromercuriphenylsulphonate. Stimulated by various salts.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=2.6 mM for naphthalene dihydrodiol (at pH 10.0); | | KM=0.9 mM for benzene dihydrodiol (at pH 10.0); | | KM=1.2 mM for 3-deoxyglucosone (at pH 7.5); | | KM=0.12 mM for camphorquinone (at pH 7.5); | | KM=1.3 mM for methylglyoxal (at pH 7.5); | | KM=6.4 mM for D-xylose (at pH 7.5); | | KM=29 mM for D-glucose (at pH 7.5); | | Vmax=36 µmol/min/mg enzyme with naphthalene dihydrodiol as substrate (at pH 10.0); | | Vmax=16 µmol/min/mg enzyme with benzene dihydrodiol as substrate (at pH 10.0); | | Vmax=17 µmol/min/mg enzyme with reduced 3-deoxyglucosone as substrate (at pH 7.5); | | Vmax=34 µmol/min/mg enzyme with camphorquinone as substrate (at pH 7.5); | | Vmax=10 µmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.5); | | Vmax=9.0 µmol/min/mg enzyme with D-xylose as substrate (at pH 7.5); | | Vmax=1.1 µmol/min/mg enzyme with D-glucose as substrate (at pH 7.5); | |
- SUBUNIT: Homodimer.
- TISSUE SPECIFICITY: Kidney.
- SIMILARITY: Belongs to the gfo/idh/mocA family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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 Feature table viewer |
| Key | From To | Length | | Description | FTId |
| CHAIN | 1 334 | 334 | | Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase. | PRO_0000315363 |
| SITE | 71 71 | 1 | | May play an important role in coenzyme binding (By similarity). | |
| SITE | 79 79 | 1 | | May play an important role in coenzyme binding. | |
| SITE | 97 97 | 1 | | May play an important role in coenzyme binding (By similarity). | |
| SITE | 176 176 | 1 | | May play an important role for the adaptation of the alcohol substrate into the binding site (By similarity). | |
| SITE | 180 180 | 1 | | May play an important role in catalytic activity. | |
| MUTAGEN | 79 79 | | | H->E: Decrease in K(d) and K(m) value for NADPH. Elimination of the fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation. Potent inhibition of the dehydrogenase activity by high ionic strength. | |
| MUTAGEN | 180 180 | | | Y->F: Significant loss of activity. No effect on the high affinity for NADPH, fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation. | |
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| Length: 334 AA [This is the length of the unprocessed precursor] |
Molecular weight: 36435 Da [This is the MW of the unprocessed precursor] |
CRC64: D319AF45660667C9 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE
70 80 90 100 110 120
LAKDPNVEVA YVGTQHPQHK AAVMLCLAAG KAVLCEKPMG VNAAEVREMV TEARSRGLFL
130 140 150 160 170 180
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLTH VPRAVDWAQA GGALLDLGIY
190 200 210 220 230 240
CVQFISMVFG GQKPEKISVM GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV
250 260 270 280 290 300
SGTKGMAQLL NPCWCPTELV VKGEHKEFLL PPVPKNCNFD NGAGMSYEAK HVRECLRKGL
310 320 330
KESPVIPLVE SELLADILEE VRRAIGVTFP QDKH
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Q7JK39 in FASTA format |
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