KEGG   ENZYME: 2.4.1.161
Entry
EC 2.4.1.161                Enzyme                                 
Name
oligosaccharide 4-alpha-D-glucosyltransferase;
amylase III;
1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glucosyltransferase;
1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase;
alpha-1,4-transglucosylase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-glucosyltransferase
Reaction(IUBMB)
Transfers the non-reducing terminal alpha-D-glucose residue from a (1->4)-alpha-D-glucan to the 4-position of a free glucose or of a glucosyl residue at the non-reducing terminus of a (1->4)-alpha-D-glucan, thus bringing about the rearrangement of oligosaccharides
Comment
The enzyme acts on amylose, amylopectin, glycogen and maltooligosaccharides. No detectable free glucose is formed, indicating the enzyme does not act as a hydrolase. The enzyme from the bacterium Cellvibrio japonicus has the highest activity with maltotriose as a donor, and also accepts maltose [3], while the enzyme from amoeba does not accept maltose [1,2]. Oligosaccharides with 1->6 linkages cannot function as donors, but can act as acceptors [3]. Unlike EC 2.4.1.25, 4-alpha-glucanotransferase, this enzyme can transfer only a single glucosyl residue.
History
EC 2.4.1.161 created 1989, modified 2013
Orthology
K18820  oligosaccharide 4-alpha-D-glucosyltransferase
Genes
VTAA0902
VNVIF132_04360
CPSCPS_0983
COMCMT41_03645
COLWA3Q33_00310
COLADBO93_10435
COVEKO29_08035
CBERB5D82_05945
LSDEMK97_14530
THATH3N35_23200 H3N35_23220
TACTSG35_024240
TVDSG34_025365 SG34_025380
PATPatl_2338
PPHEPP2015_3540
PSYMJ1N51_13205
AMCMADE_1019800
AMHI633_20510
AMAAamad1_19510
AMALI607_18470
AMAEI876_18845
AMAOI634_18610
AMADI636_18650
AMAII635_19500
AMAGI533_18545
AMACMASE_18900
AMBAMBAS45_19140
AMGAMEC673_18910
AMKAMBLS11_18205
SMAAIT774_06715
GAGGlaag_2489
GNIGNIT_2014(malZ)
GPSC427_2622
PMESFX988_00783
LALAT746_03985
CATEC2869_13950
SALHHMF8227_00575
PAEWKIH87_09635
AGZM0C34_01740
CATTOLW01_03445
PINPing_2529
FBLFbal_1099
MYAMORIYA_1778
CJACJA_3248(agd31B)
SAGAM5M_10740
MTHDA3224_13630
MICCAUP74_00400(yicI)
MAGAMag101_15405
MIIBTJ40_19695
MICTFIU95_18490(yicI)
MHYDGTQ55_15485
MCELLPW13_12975
MICZGL2_18230
MVBMJO52_18760
AFUSEYZ66_09485
WEZIC757_02340
MNRACZ75_24295
MASWAM586_15500
MTIMDIR46_24315
MASYDPH57_25600
MFYHH212_21140
MVARMasN3_31390
MASZC9I28_23705
MALIEYF70_03660
MUMFCL38_14985
MFLAGO485_10490
MPLIE1742_10795
DUGHH213_05245
UPVEJN92_03460
UNDUNDKW_1061
TCTPX653_27210
TMJP0M04_25765
TPYOX956_02300
PMETG4Y79_02790
SLRL21SP2_0552
PARYA4V02_13055
DUNFDZ78_09935
BLQL21SP5_02764(yicI)
ASXCDL62_11400
ALKQM9189_09845
MBASALGA_3015
NKONiako_7025
PSEGD3H65_19715
PGOFSB84_03440
FLSGLV81_04430
FEIK9M53_03685
FLPLK994_10835
FLCKJS93_12930
FLVKJS94_09745
RUPDTQ70_26650
HYPA0257_06410
HYHD3Y59_00775
HQIH9L05_12550
HRSHER32_03385
HMTMTP16_22500
FPFDCC35_07465
FLMMY04_2654
FLLEI427_14460
FYAKMW28_02905
FKAKM029_14945
FUVJR347_15560
FGLEM308_02215
FATDVK85_07770
FKIFK004_07435
FPALHYN49_05735
FMGHYN48_05450
FSNGS03_00955
FNKE1750_08960
FSDLXD69_07955
FLOK1I41_01935
FAZM0M57_09035
LVNBWR22_13960
POMMED152_00395
POBLPB03_00385
PRNBW723_16305
POLABXQ17_05035
POACW731_04765
PHALH9I45_00045
PLITK8354_04915
PPECH9W90_06310
PBATJL193_03310
PCEAJ3359_16910
PUNNQP51_00340
WINWPG_1776
WIJBWZ20_06900
TJETJEJU_2130
LUTLupro_12230
FOPFNB79_06045
SEONBWZ22_09275
OLLCW732_00985
OAQDZC78_08385
KOSKORDIASMS9_00835
KANIMCC3317_31660
AQBD1818_03815
AQAD1815_03760
AQDD1816_03135
PSYNE9099_09030
ANPFK178_01305
FBMMQE35_05725
SAHNJRG66_00385
CNREB819_09025
FBOJ9309_06675
SHYRLA303_03655
CPRVCYPRO_0481
 » show all
Reference
1  [PMID:2423097]
  Authors
Nebinger P.
  Title
Separation and characterization of four different amylases of Entamoeba histolytica. I. Purification and properties.
  Journal
Biol Chem Hoppe Seyler 367:161-7 (1986)
DOI:10.1515/bchm3.1986.367.1.161
Reference
2  [PMID:2423098]
  Authors
Nebinger P.
  Title
Separation and characterization of four different amylases of Entamoeba histolytica. II. Characterization of amylases.
  Journal
Biol Chem Hoppe Seyler 367:169-76 (1986)
DOI:10.1515/bchm3.1986.367.1.169
Reference
3  [PMID:23132856]
  Authors
Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, Brumer H
  Title
Structural enzymology of Cellvibrio japonicus Agd31B protein reveals alpha-transglucosylase activity in glycoside hydrolase family 31.
  Journal
J Biol Chem 287:43288-99 (2012)
DOI:10.1074/jbc.M112.416511
  Sequence
[cja:CJA_3248]
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.161
IUBMB Enzyme Nomenclature: 2.4.1.161
ExPASy - ENZYME nomenclature database: 2.4.1.161
BRENDA, the Enzyme Database: 2.4.1.161
CAS: 9000-92-4

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