2-dehydro-3-deoxyglucarate aldolase: Difference between revisions
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{{enzyme |
{{enzyme |
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| Name = 2-dehydro-3-deoxyglucarate aldolase |
| Name = 2-dehydro-3-deoxyglucarate aldolase |
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| IUBMB_EC_number = 4/1/2/20 |
| IUBMB_EC_number = 4/1/2/20 |
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| GO_code = 0008672 |
| GO_code = 0008672 |
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In [[enzymology]], a '''2-dehydro-3-deoxyglucarate aldolase''' ({{EC number|4.1.2.20}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], a '''2-dehydro-3-deoxyglucarate aldolase''' ({{EC number|4.1.2.20}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
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Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[2-dehydro-3-deoxy-D-glucarate]], and two [[product (chemistry)|products]], [[pyruvate]] and [[tartronate semialdehyde]]. |
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[2-dehydro-3-deoxy-D-glucarate]], and two [[product (chemistry)|products]], [[pyruvate]] and [[tartronate semialdehyde]]. |
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This enzyme belongs to the family of [[lyase]]s, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is '''2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase (pyruvate-forming)'''. Other names in common use include '''2-keto-3-deoxyglucarate aldolase''', '''alpha-keto-beta-deoxy-D-glucarate aldolase''', and '''2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase'''. This enzyme participates in [[ascorbate and aldarate metabolism]]. |
This enzyme belongs to the family of [[lyase]]s, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is '''2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase (pyruvate-forming)'''. Other names in common use include '''2-keto-3-deoxyglucarate aldolase''', '''alpha-keto-beta-deoxy-D-glucarate aldolase''', and '''2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase'''. This enzyme participates in [[ascorbate and aldarate metabolism]]. |
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==Structural studies== |
==Structural studies== |
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==References== |
==References== |
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{{Reflist|1}} |
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* {{cite journal | author = Fish DC and Blumenthal HJ | date = 1966 | title = 2-Keto-3-deoxy-D-glucarate aldolase | journal = Methods Enzymol. | volume = 9 | pages = 529–534 | doi = 10.1016/0076-6879(66)09105-5 | chapter = [93] 2-Keto-3-deoxy-d-glucarate aldolase☆☆☆ | series = Methods in Enzymology | isbn = 9780121818098 }} |
* {{cite journal | author = Fish DC and Blumenthal HJ | date = 1966 | title = 2-Keto-3-deoxy-D-glucarate aldolase | journal = Methods Enzymol. | volume = 9 | pages = 529–534 | doi = 10.1016/0076-6879(66)09105-5 | chapter = [93] 2-Keto-3-deoxy-d-glucarate aldolase☆☆☆ | series = Methods in Enzymology | isbn = 9780121818098 }} |
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[[Category:EC 4.1.2]] |
[[Category:EC 4.1.2]] |
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[[Category:Enzymes of known structure]] |
[[Category:Enzymes of known structure]] |
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Revision as of 08:24, 7 October 2011
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| 2-dehydro-3-deoxyglucarate aldolase | |||||||||
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| Identifiers | |||||||||
| EC no. | 4.1.2.20 | ||||||||
| CAS no. | 37290-56-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 2-dehydro-3-deoxyglucarate aldolase (EC 4.1.2.20) is an enzyme that catalyzes the chemical reaction
- 2-dehydro-3-deoxy-D-glucarate pyruvate + tartronate semialdehyde
Hence, this enzyme has one substrate, 2-dehydro-3-deoxy-D-glucarate, and two products, pyruvate and tartronate semialdehyde.
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase (pyruvate-forming). Other names in common use include 2-keto-3-deoxyglucarate aldolase, alpha-keto-beta-deoxy-D-glucarate aldolase, and 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1DXE, 1DXF, 1W37, 1W3I, 1W3N, and 1W3T.
References
- Fish DC and Blumenthal HJ (1966). "2-Keto-3-deoxy-D-glucarate aldolase". Methods Enzymol. Methods in Enzymology. 9: 529–534. doi:10.1016/0076-6879(66)09105-5. ISBN 9780121818098.
{{cite journal}}:|chapter=ignored (help)