|
Your query returned 7 entries. Printable version
EC | 1.1.1.263 | ||||||||||||||
Accepted name: | 1,5-anhydro-D-fructose reductase | ||||||||||||||
Reaction: | 1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+ | ||||||||||||||
Systematic name: | 1,5-anhydro-D-glucitol:NADP+ oxidoreductase | ||||||||||||||
Comments: | Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 206138-19-4 | ||||||||||||||
References: |
| ||||||||||||||
EC | 1.1.1.292 | ||||||||||||||
Accepted name: | 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) | ||||||||||||||
Reaction: | 1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH + H+ | ||||||||||||||
Other name(s): | 1,5-anhydro-D-fructose reductase (ambiguous); AFR (ambiguous) | ||||||||||||||
Systematic name: | 1,5-anhydro-D-mannitol:NADP+ oxidoreductase | ||||||||||||||
Comments: | This enzyme is present in some but not all Rhizobium species and belongs in the GFO/IDH/MocA protein family [2]. This enzyme differs from hepatic 1,5-anhydro-D-fructose reductase, which yields 1,5-anhydro-D-glucitol as the product (see EC 1.1.1.263). In Sinorhizobium morelense, the product of the reaction, 1,5-anhydro-D-mannitol, can be further metabolized to D-mannose [1]. The enzyme also reduces 1,5-anhydro-D-erythro-hexo-2,3-diulose and 2-ketoaldoses (called osones), such as D-glucosone (D-arabino-hexos-2-ulose) and 6-deoxy-D-glucosone. It does not reduce common aldoses and ketoses, or non-sugar aldehydes and ketones [1]. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
References: |
| ||||||||||||||
EC | 4.2.1.110 | ||||||||||||||
Accepted name: | aldos-2-ulose dehydratase | ||||||||||||||
Reaction: | 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
+ H2O (overall reaction) (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one |
||||||||||||||
For diagram of the anhydrofructose pathway, click here | |||||||||||||||
Glossary: | 1,5-anhydro-D-fructose = 1,5-anhydro-D-arabino-hex-2-ulose = (4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)dihydro-2H-pyran-3(4H)-one ascopyrone M = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = (6S)-4-hydroxy-6-(hydroxymethyl)-2H-pyran-3(6H)-one microthecin = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one |
||||||||||||||
Other name(s): | pyranosone dehydratase; AUDH; 1,5-anhydro-D-fructose dehydratase (microthecin-forming) | ||||||||||||||
Systematic name: | 1,5-anhydro-D-fructose hydro-lyase (microthecin-forming) | ||||||||||||||
Comments: | This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly [1,2,4]. This is a bifunctional enzyme that acts as both a lyase and as an isomerase [2]. Differs from EC 4.2.1.111, which can carry out only reaction (1a), is inhibited by its product and requires metal ions for activity [1]. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 101920-80-3 | ||||||||||||||
References: |
| ||||||||||||||
EC | 4.2.1.111 | ||||||||||||||
Accepted name: | 1,5-anhydro-D-fructose dehydratase | ||||||||||||||
Reaction: | 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O | ||||||||||||||
For diagram of the anhydrofructose pathway, click here | |||||||||||||||
Glossary: | 1,5-anhydro-D-fructose = 1,5-anhydro-D-arabino-hex-2-ulose = (4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)dihydro-2H-pyran-3(4H)-one ascopyrone M = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = (6S)-4-hydroxy-6-(hydroxymethyl)-2H-pyran-3(6H)-one |
||||||||||||||
Other name(s): | 1,5-anhydro-D-fructose 4-dehydratase; 1,5-anhydro-D-fructose hydrolyase; 1,5-anhydro-D-arabino-hex-2-ulose dehydratase; AFDH; AF dehydratase; 1,5-anhydro-D-fructose hydro-lyase | ||||||||||||||
Systematic name: | 1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming) | ||||||||||||||
Comments: | This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.2.13 [exo-(1→4)-α-D-glucan lyase] and EC 5.3.2.7 (ascopyrone tautomerase). Requires divalent (Ca2+ or Mg2+) or monovalent cations (Na+) for optimal activity. Unlike EC 4.2.1.110, the enzyme is specific for 1,5-anhydro-D-fructose as substrate and shows no activity towards aldose-2-uloses such as 2-dehydroglucose [1,2,3]. In addition, it is inhibited by its end-product ascopyrone M [2] and it cannot convert ascopyrone M into microthecin, as can EC 4.2.1.110. | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
| ||||||||||||||
EC | 4.2.2.13 | ||||||||||||||
Accepted name: | exo-(1→4)-α-D-glucan lyase | ||||||||||||||
Reaction: | linear α-glucan = (n-1) 1,5-anhydro-D-fructose + D-glucose | ||||||||||||||
For diagram of the anhydrofructose pathway, click here | |||||||||||||||
Other name(s): | α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase; α-1,4-glucan exo-lyase; α-1,4-glucan lyase; GLase | ||||||||||||||
Systematic name: | (1→4)-α-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming) | ||||||||||||||
Comments: | The enzyme catalyses the sequential degradation of (1→4)-α-D-glucans from the non-reducing end with the release of 1,5-anhydro-D-fructose. Thus, for an α-glucan containing n (1→4)-linked glucose units, the final products are 1 glucose plus (n-1) 1,5-anhydro-D-fructose. Maltose, maltosaccharides and amylose are all completely degraded. It does not degrade (1→6)-α-glucosidic bonds and thus the degradation of a branched glucan, such as amylopectin or glycogen, will result in the formation of 1,5-anhydro-D-fructose plus a limit dextrin. Other enzymes involved in the anhydrofructose pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 5.3.2.7 (ascopyrone tautomerase). | ||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 148710-18-3 | ||||||||||||||
References: |
| ||||||||||||||
EC | 5.3.2.7 | ||||||||||||||
Accepted name: | ascopyrone tautomerase | ||||||||||||||
Reaction: | 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose | ||||||||||||||
For diagram of the anhydrofructose pathway, click here | |||||||||||||||
Glossary: | ascopyrone M = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = (6S)-4-hydroxy-6-(hydroxymethyl)-2H-pyran-3(6H)-one ascopyrone P = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose = (2S)-5-hydroxy-2-(hydroxymethyl)-2H-pyran-4(3H)-one |
||||||||||||||
Other name(s): | ascopyrone isomerase; ascopyrone intramolecular oxidoreductase; 1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase; APM tautomerase; ascopyrone P tautomerase; APTM | ||||||||||||||
Systematic name: | 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose Δ3-Δ1-isomerase | ||||||||||||||
Comments: | This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 4.2.2.13 [exo-(1→4)-α-D-glucan lyase]. Ascopyrone P is an anti-oxidant [2]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
| ||||||||||||||
EC | 5.3.3.15 | ||||||||||||||
Transferred entry: | ascopyrone tautomerase. Now EC 5.3.2.7, ascopyrone tautomerase | ||||||||||||||