1.1.1.282: quinate/shikimate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about quinate/shikimate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.282
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1.1.1.282
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3-dehydroquinate
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lignin
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corynebacterium
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nad+-dependent
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glutamicum
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cosubstrate
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drug development
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dehydrogenases
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agriculture
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synthesis
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medicine
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pharmacology
- 1.1.1.282
- 3-dehydroquinate
- lignin
-
corynebacterium
-
nad+-dependent
- glutamicum
-
cosubstrate
- drug development
- dehydrogenases
- agriculture
- synthesis
- medicine
- pharmacology
Reaction
Synonyms
cgl0424, cgR_0495, dehydroquinate dehydratase-shikimate dehydrogenase, More, NAD+ cofactor-specific QDH, NAD+-dependent enzyme quinate/shikimate dehydrogenase, NADP+ cofactor-specific QDH, NADP+-specific DHQD-QDH, PintaQDH, Poptr2, Poptr3, Poptr4, QDH, QSDH, qsuD, quinate dehydrogenase, quinate/shikimate 5-dehydrogenase, quinate/shikimate dehydrogenase, rifI, RifI2, SDH, SDH/QDH, sdhL, shikimate/quinate dehydrogenase, YdiB
ECTree
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Cofactor
Cofactor on EC 1.1.1.282 - quinate/shikimate dehydrogenase [NAD(P)+]
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3-acetylpyridine adenine dinucleotide
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67% of the activity with NAD+
nicotinamide 1,N6-ethenoadenine dinucleotide
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69% of the activity with NAD+
nicotinamide hypoxanthine dinucleotide
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1.3fold higher activity than with NAD+
NAD+
NAD+ binding site, bound very tightly, NAD+ is bound to the Rossmann domain in an elongated fashion with the nicotinamide ring in the pro-R conformation, specificity for binding NAD+ over NADP+
NAD+
utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding
NAD+
the C-terminal domain of each protomer in the RifI2 asymmetric unit contains a bound molecule of NAD+, Cofactor binding structure and mechanism, detailed overview
NADP+
utilizes either NAD+ or NADP+ as a cofactor, tendency to be more efficient with NAD+ than with NADP+, mode of binding
additional information
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absolute requirement for a nicotinamide nucleotide cofactor for the oxidation of quinate or shikimate, cofactor specificity, not: alpha-NAD+, beta-NMN or nicotinic acid dinucleotide
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additional information
CglQSDH is strictly NAD(H)-dependent due to structural features
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additional information
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CglQSDH is strictly NAD(H)-dependent due to structural features
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additional information
in the RifI2 structure, the NADP+-specifying motif is replaced with Asp-Pro-Ser-Thr-Ala-Arg (residues 156-161). The side chain of Asp156 binds to the adenine ribose of NAD+, while its negative charge is predicted to repel the additional phosphate of NADP+. RifI2 possesses low apparent binding affinity for NADP+. Analysis of the cofactor-binding sites of the RifI2NAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview
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additional information
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in the RifI2 structure, the NADP+-specifying motif is replaced with Asp-Pro-Ser-Thr-Ala-Arg (residues 156-161). The side chain of Asp156 binds to the adenine ribose of NAD+, while its negative charge is predicted to repel the additional phosphate of NADP+. RifI2 possesses low apparent binding affinity for NADP+. Analysis of the cofactor-binding sites of the RifI2NAD+ complex and structure comparison, inportance of the invariant residue Asn193 in the cofactor-binding site, overview
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additional information
the turnover number is lower with NADP+ instead of NAD+ as cofactor. NADP(H) is just only for 3-dehydroquinate reduction by the enzyme
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