KEGG   ENZYME: 1.1.99.31Help
Entry
EC 1.1.99.31                Enzyme                                 

Name
(S)-mandelate dehydrogenase;
MDH
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
(S)-mandelate:acceptor 2-oxidoreductase
Reaction(IUBMB)
(S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor [RN:R03793]
Reaction(KEGG)
R03793 > R07664;
(other) R04160
Show
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
KPZ: KPNIH27_29500
KPK: A593_26110
EBC: C2U52_20660
SRR: SerAS9_2024
SRL: SOD_c18970(mdlB)
SRY: M621_10465
SPLY: Q5A_010505(mdlB_2)
SRS: SerAS12_2024
SRA: SerAS13_2025
SERA: Ser39006_008175
RAA: Q7S_10965
PLU: plu1106
PMK: MDS_0258
PPUN: PP4_48090
PSIL: PMA3_26255
MBS: MRBBS_1292(mdlB)
GAI: IMCC3135_15650(mdlB_1)
CSA: Csal_1075
HEL: HELO_1144
HAM: HALO3110
REH: H16_B1832(mdlB)
CNC: CNE_2c17870(mdlB) CNE_BB1p09340(lldA)
BOK: DM82_843(mdlB)
BOC: BG90_87(mdlB)
BGU: KS03_3099(mdlB)
BGO: BM43_2882(mdlB)
BYI: BYI23_D002250(mdlB)
BUE: BRPE67_DCDS04000(mdlB)
BGP: BGL_1c14480(mdlB)
BXE: Bxe_B0136
BXB: DR64_5486(mdlB)
BFN: OI25_63(mdlB)
PPNO: DA70_09870
PPNM: LV28_21225
PPUL: RO07_15460
PSPU: NA29_21610
PAPI: SG18_24535
BBR: BB1109(lldD)
BBM: BN115_1055(lldD)
BBH: BN112_2341(lldD)
BBX: BBS798_1077(lldD)
BHO: D560_0958(mdlB)
BHM: D558_0941(mdlB)
AXX: ERS451415_05599(mdlB_4)
PNA: Pnap_1020
HSE: Hsero_0244(lldD)
HRB: Hrubri_0228(lldD) Hrubri_1083(mdlB)
AZO: azo2470(lldD)
AZA: AZKH_1692(lldD) AZKH_1885
AOA: dqs_2614
BJA: bll6401
SNO: Snov_4068
MSC: BN69_3477
PDE: Pden_5045
CID: P73_2967
SWI: Swit_4230
AAY: WYH_00438(mdlB)
MAGX: XM1_4569
REQ: REQ_43160
 » show all
Taxonomy
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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