KEGG   ENZYME: 1.1.99.31
Entry
EC 1.1.99.31                Enzyme                                 
Name
(S)-mandelate dehydrogenase;
MDH (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
Sysname
(S)-mandelate:acceptor 2-oxidoreductase
Reaction(IUBMB)
(S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor [RN:R03793]
Reaction(KEGG)
R03793 > R07664;
(other) R04160
Substrate
(S)-mandelate [CPD:C01984];
acceptor [CPD:C00028]
Product
phenylglyoxylate [CPD:C02137];
reduced acceptor [CPD:C00030]
Comment
This enzyme is a member of the FMN-dependent alpha-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3].
History
EC 1.1.99.31 created 2006
Pathway
ec00627  Aminobenzoate degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K15054  (S)-mandelate dehydrogenase
Genes
KPZKPNIH27_29500
KPKA593_26110
KINAB182_10085
PDZHHA33_12690
METYMRY16398_22310(lldD)
EBCC2U52_20660
SRRSerAS9_2024
SRLSOD_c18970(mdlB)
SRYM621_10465
SPLYQ5A_010505(mdlB_2)
SRSSerAS12_2024
SRASerAS13_2025
RAHRahaq_2166
RACEJHW33_05990
RAQRahaq2_2270
RAAQ7S_10965
ROXBV494_06240
PRODPCO85_17630
SERASer39006_008175
SERQCWC46_08170
PAOPat9b_5751
TCIA7K98_03450 A7K98_09625
PLUplu1106
PLUMA4R40_05455
PMKMDS_0258
PPUNPP4_48090
PMUDNCTC8068_03334(mdlB)
PLULFOB45_03525
PSILPMA3_26255
PALLUYA_00945
PSEJHNQ25_00355
PTYJWV26_11420
PKMPZ739_14425 PZ739_27740
AVIVLF296_07290
GAIIMCC3135_15650(mdlB_1)
CSACsal_1075
CCAGSR908_12925
HELHELO_1144
HAKKO116_03908
HHUAR456_15730
HTTHZS52_06555
HPROLMS44_22910
HBHE4T21_15460
HHAOQWG60_01075
KUYFY550_01725
MGEOCFI10_09980
RPJN234_37865
REHH16_B1832(mdlB)
CNCCNE_2c17870(mdlB) CNE_BB1p09340(lldA)
REUReut_B3845 Reut_C6258
CUKKB879_14195
BCEPAPZ15_29795
BSEMWJ12_27655 WJ12_29785
BGLbglu_1g22680
BGUKS03_3099(mdlB)
BUGBC1001_0562
BGFBC1003_4245 BC1003_5931 BC1003_6041
BGDbgla_1g16560
BGOBM43_2882(mdlB)
BYIBYI23_D002250(mdlB)
BUEBRPE67_DCDS04000(mdlB)
BUQAC233_22965
BGPBGL_1c14480(mdlB)
BPLAbpln_1g14030
BUMAXG89_31730 AXG89_36055
BUIAX768_16445
BURKDM992_18225
BXEBxe_B0136
BXBDR64_5486(mdlB)
BPHBphy_5156 Bphy_6162
BGEBC1002_6152
BPXBUPH_04446 BUPH_04485
BFNOI25_63(mdlB)
PSPWBJG93_28250
PHSC2L64_43710
PCAFDSC91_002503
PMEGFNZ07_00035
PACSFAZ98_17720 FAZ98_33820
PPKU875_17400
PPNODA70_09870
PPNMLV28_21225
PRBX636_17015
PPULRO07_15460
PSPUNA29_21610
PAPISG18_24535
PVEUC34_06685
POXMB84_11135
PFGAB870_17715
PNRAT302_00440
PANDDRB87_06060
PFIBPI93_021585
PCOMNTU39_07595
CABASBC2_42390(mdlB)
CABKNK8_62260 NK8_73200 NK8_77950
TVLFAZ95_29925
BBHBN112_2341(lldD)
BBRBB1109(lldD)
BBMBN115_1055(lldD)
BBXBBS798_1077(lldD)
BHOD560_0958(mdlB)
BHZACR54_02380(mdlB_2)
BFZBAU07_00075
BPDZBBN53_10075
BGMCAL15_19635
BOJCBF45_00085
BGVCAL12_00090
AXONH44784_012131 NH44784_027291
AXNAX27061_0944 AX27061_5576
AXXERS451415_00929(mdlB_1) ERS451415_05599(mdlB_4)
ADTAPT56_25710
AISBUW96_08255
ADYHLG70_24245
APESFOC84_27045
AAEGRA224_14795
AAQUD3M96_18515
AAMMFE795_16070
BOZDBV39_02620
PIGEGT29_08500 EGT29_27015
PACRFXN63_01975 FXN63_24830
KGYEHF36_00220
PARKLSG25_18645
NARMN7E01_09140
RHYRD110_17475 RD110_22745
PNAPnap_1020
ACKC380_23560
ATEMPQV96_14425
VAPVapar_3912
VPDVAPA_2c12340
VAMC4F17_30270
HYNF9K07_00635 F9K07_07145
HCZG9Q37_10890
HSEHsero_0244(lldD)
HSZACP92_01205
HRBHrubri_0228(lldD) Hrubri_1083(mdlB)
HFRG5S34_01060
GLCJQN73_20910
APETToN1_43340
AZOazo2470(lldD)
AOAdqs_2614
AZAAZKH_1692(lldD) AZKH_1885
AZIAzCIB_1257
AZDCDA09_08695 CDA09_10570
AZRCJ010_15385
TMZTmz1t_0668
TCLTchl_0094 Tchl_1486
THKCCZ27_17095
TAKTharo_0088 Tharo_3014
MESRFGU64_10705
MESOBSQ44_18490
RTRRTCIAT899_PC05950
RHRCKA34_03290 CKA34_26460
RBQJ2J99_03850
ARAArad_12221
NGLRG1141_CH38130
NGGRG540_CH38780
NPMQEO92_29565
BJAbll6401(bll6401)
BBRAQA636_07320 QA636_07380
MSCBN69_3477
MPARF7D14_04315
LABTFIU93_07200(mdlB)
CIDP73_2967
CEHCEW89_13885
PABYGa0080574_TMP2102
SUALKDD17_04355
TRYQF118_09660
RMAIMACH21_21460
TSCOR1T40_02130
RBXI3V23_13085
SWISwit_4230
SPYGYGS_C1P2754
SPZRG5C33_10880
PMASNCF86_11405
CMANA9D14_18035
ERYCP97_05395
AOZHUE56_26160
SKTIGS68_08990
SMUCJL100_018390
SROEJL101_017090
MAGXXM1_4569
PDEFP9209_06030
ARHDVSH64_10230
SMAMMal15_65410(mdlB)
CHRJCHRYMOREF3P_1132
 » show all
Reference
1  [PMID:10231535]
  Authors
Lehoux IE, Mitra B.
  Title
(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.
  Journal
Biochemistry 38:5836-48 (1999)
DOI:10.1021/bi990024m
Reference
2  [PMID:15311930]
  Authors
Dewanti AR, Xu Y, Mitra B.
  Title
Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity.
  Journal
Biochemistry 43:10692-700 (2004)
DOI:10.1021/bi049005p
Reference
3  [PMID:14967029]
  Authors
Dewanti AR, Xu Y, Mitra B.
  Title
Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism.
  Journal
Biochemistry 43:1883-90 (2004)
DOI:10.1021/bi036021y
Other DBs
ExplorEnz - The Enzyme Database: 1.1.99.31
IUBMB Enzyme Nomenclature: 1.1.99.31
ExPASy - ENZYME nomenclature database: 1.1.99.31
UM-BBD (Biocatalysis/Biodegradation Database): 1.1.99.31
BRENDA, the Enzyme Database: 1.1.99.31
CAS: 9067-95-2
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