KEGG   ENZYME: 2.4.1.231
Entry
EC 2.4.1.231                Enzyme                                 
Name
alpha,alpha-trehalose phosphorylase (configuration-retaining);
trehalose phosphorylase[ambiguous]
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
alpha,alpha-trehalose:phosphate alpha-D-glucosyltransferase
Reaction(IUBMB)
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate [RN:R07265]
Reaction(KEGG)
R07265
Substrate
alpha,alpha-trehalose [CPD:C01083];
phosphate [CPD:C00009]
Product
alpha-D-glucose [CPD:C00267];
alpha-D-glucose 1-phosphate [CPD:C00103]
Comment
Unlike EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
History
EC 2.4.1.231 created 2003
Orthology
K22248  alpha,alpha-trehalose phosphorylase (configuration-retaining)
Genes
NCRNCU09559(ccg-9)
NTENEUTE1DRAFT131038(NEUTE1DRAFT_131038)
SMPSMAC_05699(putative ccg9)
PANPODANSg1171
TTTTHITE_2117861
MTMMYCTH_2308065
CTHRCTHT_0019540
MGRMGG_00195
TMNUCRPA7_8792
SSCKSPSK_08651
FGRFGSG_04456
FPUFPSE_09908
FVRFVEG_11189
FOXFOXG_07014 FOXG_13755 FOXG_14686
NHENECHADRAFT_123394
TRETRIREDRAFT_121491
TRRM419DRAFT_122799
MAWMAC_09793
MAJMAA_09323
PLJVFPFJ_06499 VFPFJ_09736
VALVDBG_02869
VDAVDAG_03780
CFJCFIO01_02532
ELAUCREL1_294
PFYPFICI_08469
MBEMBM_07660
PSCOLY89DRAFT_588035
GLZGLAREA_02452
ANIAN4128.2 AN5021.2
AFMAFUA_3G12100 AFUA_5G14780
ACTACLA_039960 ACLA_097070
NFINFIA_065220
AORAO090003000770 AO090103000417
ANGANI_1_1116164(An18g01640) ANI_1_2720024(An02g07770)
AFVAFLA_000910 AFLA_013117
ALUCAKAW2_10646A AKAW2_31399A
ACHEACHE_21207S
APUUAPUU_10466S APUU_30758A
PCSPc18g00270
PDPPDIP_75450
TMFPMAA_021000
TRGTRUGW13939_04300 TRUGW13939_10499
CIMCIMG_11719(CIMG06287)
CPWCPC735_028170
UREUREG_04096
PBLPAAG_08074
PBNPADG_08386
ABEARB_07071
TVETRV_05695
AJEHCAG_06976
BGHBDBG_05838
PNOSNOG_09339
PTEPTT_04389
BZECOCCADRAFT_30642
BSCCOCSADRAFT_197298
BORCOCMIDRAFT_2158
AALTCC77DRAFT_934424
BCOMBAUCODRAFT_78356
NPAUCRNP2_8457
CNECNG04480
CNBCNBG0220
CGICGB_G0190C
TMSTREMEDRAFT_36511
TVSTRAVEDRAFT_28241
DSQDICSQDRAFT_135570
PCOPHACADRAFT_144860
SHSSTEHIDRAFT_145406
HIRHETIRDRAFT_146007
PSQPUNSTDRAFT_104328 PUNSTDRAFT_134729
ADLAURDEDRAFT_142012
FMEFOMMEDRAFT_104325
GTRGLOTRDRAFT_122804 GLOTRDRAFT_137277
MPRMPER_08488
MRRMoror_6467
CCICC1G_03906
SCMSCHCODRAFT_10496
ABPAGABI1DRAFT111552(AGABI1DRAFT_111552)
ABVAGABI2DRAFT190782(AGABI2DRAFT_190782)
SLASERLADRAFT_351395
NGDNGA_2006900
KBSEPA93_17535
MIBUY43_C0001G0046
 » show all
Reference
1  [PMID:11931662]
  Authors
Eis C, Nidetzky B.
  Title
Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors.
  Journal
Biochem J 363:335-40 (2002)
DOI:10.1042/0264-6021:3630335
Reference
2  [PMID:11389683]
  Authors
Eis C, Watkins M, Prohaska T, Nidetzky B.
  Title
Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune.
  Journal
Biochem J 356:757-67 (2001)
DOI:10.1042/0264-6021:3560757
Reference
3  [PMID:11736665]
  Authors
Nidetzky B, Eis C.
  Title
Alpha-retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors.
  Journal
Biochem J 360:727-36 (2001)
DOI:10.1042/0264-6021:3600727
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.231
IUBMB Enzyme Nomenclature: 2.4.1.231
ExPASy - ENZYME nomenclature database: 2.4.1.231
BRENDA, the Enzyme Database: 2.4.1.231
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