| EC |
3.2.1.202 |
| Accepted name: |
endo-chitodextinase |
| Reaction: |
Hydrolysis of chitodextrins, releasing N,N′-diacetylchitobiose and small amounts of N,N′,N′′-triacetylchitotriose. |
| Other name(s): |
endo I (gene name); chitodextrinase (ambiguous); endolytic chitodextrinase; periplasmic chitodextrinase |
| Systematic name: |
(1→4)-2-acetamido-2-deoxy-β-D-glucan diacetylchitobiohydrolase (endo-cleaving) |
| Comments: |
The enzyme, characterized from the bacterium Vibrio furnissii, is an endo-cleaving chitodextrinase that participates in the the chitin catabolic pathway found in members of the Vibrionaceae. Unlike EC 3.2.1.14, chitinase, it has no activity on chitin. The smallest substrate is a tetrasaccharide, and the final products are N,N′-diacetylchitobiose and small amounts of N,N′,N′′-triacetylchitotriose. cf. EC 3.2.1.200, exo-chitinase (non-reducing end), and EC 3.2.1.201, exo-chitinase (reducing end). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Bassler, B.L., Yu, C., Lee, Y.C. and Roseman, S. Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J. Biol. Chem. 266 (1991) 24276–24286. [PMID: 1761533] |
| 2. |
Keyhani, N.O. and Roseman, S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase. J. Biol. Chem. 271 (1996) 33414–33424. [DOI] [PMID: 8969204] |
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| [EC 3.2.1.202 created 2017] |
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