This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Degradation/Utilization/Assimilation → Carbohydrates Degradation → Sugars Degradation → Trehalose Degradation|
Some taxa known to possess this pathway include : Asanoa ferruginea, Bradyrhizobium japonicum, Euglena gracilis, Flammulina velutipes, Geobacillus stearothermophilus, Kocuria varians, Plesiomonas sp. Yoshida 95, Scytonema sp., Thermoanaerobacter brockii
There are several alternative pathways for the degradation of trehalose. Depending on the organism, trehalose may enter the cell either through a permease, in which case it remains unmodified, or it may be transported by a phosphotransferase system (PTS), resulting in the phoshorylated trehalose-6-phosphate form. Degradation then proceeds by different mechanisms: Unmodified trehalose may be degraded by a hydrolyzing trehalase (see trehalose degradation II (trehalase)), or it may be split by the action of a trehalose phosphorylase (see trehalose degradation IV and trehalose degradation V). Likewise, trehalose-6-phosphate may be either hydrolyzed by trehalose-6-phosphate hydrolase (see trehalose degradation I (low osmolarity)) or it could be attacked by a trehalose-6-phosphate phosphorylase (see trehalose degradation III).
About This Pathway
Two varieties of TP enzymes have been characterized: One variety is specific for the α forms of D-glucose and D-glucose-1-phosphate, while the other is specific for the β forms. Thus, the two forms catalyze different reactions, and were given different EC numbers (see the pathway trehalose degradation V for the enzymes that use the α form). The glucose-1-phosphate that is formed by the phosphorylase during trehalose degradation is subsequently converted to glucose-6-phosphate by the appropriate phosphoglucomutase (which is also either α- or β-specific).
β-specific TP enzymes have been found in various organisms, including the green algae Euglena gracilis [Belocopitow70, Marechal72], and various bacteria, including Geobacillus stearothermophilus [Inoue02, Inoue02a], Asanoa ferruginea [Aisaka98, Aisaka95], Thermoanaerobacter brockii, Plesiomonas sp. Yoshida 95 [Yoshida95], Bradyrhizobium japonicum and the cyanobacterium Scytonema sp. [PageSharp99].
Aisaka98: Aisaka K, Masuda T, Chikamune T, Kamitori K (1998). "Purification and characterization of trehalose phosphorylase from Catellatospora ferruginea." Biosci Biotechnol Biochem 62(4);782-7. PMID: 9614710
Inoue02: Inoue Y, Yasutake N, Oshima Y, Yamamoto Y, Tomita T, Miyoshi S, Yatake T (2002). "Cloning of the maltose phosphorylase gene from Bacillus sp. strain RK-1 and efficient production of the cloned gene and the trehalose phosphorylase gene from Bacillus stearothermophilus SK-1 in Bacillus subtilis." Biosci Biotechnol Biochem 66(12);2594-9. PMID: 12596853
Inoue02a: Inoue Y, Ishii K, Tomita T, Yatake T, Fukui F (2002). "Characterization of trehalose phosphorylase from Bacillus stearothermophilus SK-1 and nucleotide sequence of the corresponding gene." Biosci Biotechnol Biochem 66(9);1835-43. PMID: 12400680
Marechal72: Marechal LR, Belocopitow E (1972). "Metabolism of trehalose in Euglena gracilis. I. Partial purification and some properties of trehalose phosphorylase." J Biol Chem 247(10);3223-8. PMID: 4623846
PageSharp99: Page-Sharp M, Behm CA, Smith GD (1999). "Involvement of the compatible solutes trehalose and sucrose in the response to salt stress of a cyanobacterial Scytonema species isolated from desert soils." Biochim Biophys Acta 1472(3);519-28. PMID: 10564766
Yoshida95: Yoshida M, Nakamura N, Horikoshi K (1995). "Production and application of maltose phosphorylase and trehalose phosphorylase by a strain of Plesiomonas (In Japanese)." Oyo Toshitsu Kagaku 42:19–25.
Belocopitow74: Belocopitow E, Marechal LR (1974). "Metabolism of trehalose in Euglena gracilis. Partial purification and some properties of phosphoglucomutase acting on beta-glucose 1-phosphate." Eur J Biochem 46(3);631-7. PMID: 4212162
Crowe94: Crowe LM, Spargo BJ, Ioneda T, Beaman BL, Crowe JH (1994). "Interaction of cord factor (alpha, alpha'-trehalose-6,6'-dimycolate) with phospholipids." Biochim Biophys Acta 1194(1);53-60. PMID: 8075141
Curtis75: Curtis SJ, Epstein W (1975). "Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase." J Bacteriol 122(3);1189-99. PMID: 1097393
Dai06: Dai J, Wang L, Allen KN, Radstrom P, Dunaway-Mariano D (2006). "Conformational cycling in beta-phosphoglucomutase catalysis: reorientation of the beta-D-glucose 1,6-(Bis)phosphate intermediate." Biochemistry 45(25);7818-24. PMID: 16784233
Dai99: Dai N, Schaffer A, Petreikov M, Shahak Y, Giller Y, Ratner K, Levine A, Granot D (1999). "Overexpression of Arabidopsis hexokinase in tomato plants inhibits growth, reduces photosynthesis, and induces rapid senescence." Plant Cell 11(7);1253-66. PMID: 10402427
Giese05: Giese JO, Herbers K, Hoffmann M, Klosgen RB, Sonnewald U (2005). "Isolation and functional characterization of a novel plastidic hexokinase from Nicotiana tabacum." FEBS Lett 579(3);827-31. PMID: 15670855
Hansen03: Hansen T, Schonheit P (2003). "ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity." FEMS Microbiol Lett 226(2);405-11. PMID: 14553940
Helfert95: Helfert C, Gotsche S, Dahl MK (1995). "Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a phospho-alpha-(1-1)-glucosidase encoded by the treA gene." Mol Microbiol 16(1);111-120. PMID: 7651129
Jung14: Jung JH, Seo DH, Holden JF, Park CS (2014). "Identification and Characterization of an Archaeal Kojibiose Catabolic Pathway in the Hyperthermophilic Pyrococcus sp. Strain ST04." J Bacteriol 196(5);1122-31. PMID: 24391053
Kuznetsova06: Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF (2006). "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family." J Biol Chem 281(47):36149-61. PMID: 16990279
Showing only 20 references. To show more, press the button "Show all references".
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493