Entry
Name
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH);
Pyr2C reductase;
1,2-didehydropipecolate reductase;
P2C reductase;
1,2-didehydropipecolic reductase;
DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous);
L-pipecolate:NADP+ 2-oxidoreductase;
DELTA1-piperideine-2-carboxylate reductase;
Delta1-piperideine-2-carboxylate reductase
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-pipecolate/L-proline:NADP+ 2-oxidoreductase
Reaction(IUBMB)
(1) L-pipecolate + NADP+ = 1-piperideine-2-carboxylate + NADPH + H+ [RN:
R02203 ];
(2) L-proline + NADP+ = 1-pyrroline-2-carboxylate + NADPH + H+ [RN:
R01249 ]
Reaction(KEGG)
Substrate
Product
Comment
The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC
1.5.1.1 , 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.
History
EC 1.5.1.21 created 1984 (EC 1.5.1.14 created 1976, incorporated 1989), modified 2015
Pathway
ec00960 Tropane, piperidine and pyridine alkaloid biosynthesis
Orthology
K13609 delta1-piperideine-2-carboxylate reductase
Genes
RTG : NCTC13098_06399(ybiC_3)
KIE : NCTC12125_03109(ybiC)
SFJ : SAMEA4384070_1859(ybiC_1)
PFUW : KF707C_2150 KF707C_24890
PFUV : NLK61_00855 NLK61_04890
PFL : PFL_1416 PFL_2200 PFL_2905
PPRC : PFLCHA0_c14530 PFLCHA0_c22600 PFLCHA0_c29510
PPRO : PPC_1470 PPC_2240 PPC_2937
PMUD : NCTC8068_02634(ybiC)
PCH : EY04_06365 EY04_13730
PCZ : PCL1606_31970 PCL1606_46950
PCP : JM49_16210 JM49_23270
PCHP : C4K32_1489 C4K32_2949
PFZ : AV641_10885 AV641_13400
PALK : PSAKL28_27760 PSAKL28_28750
PSEM : TO66_07035 TO66_14500
PSOS : POS17_1439 POS17_2151 POS17_3175
PFK : PFAS1_24845 PFAS1_26870
PUM : HGP31_13870 HGP31_16480
PPSH : G5J76_12940 G5J76_14145
PSEP : C4K39_2523 C4K39_5176 C4K39_5251
PPII : QL104_07770 QL104_11580 QL104_16650
PVW : HU752_014575 HU752_024125
PQI : KH389_13730 KH389_15905
PAZE : KSS91_13490 KSS91_13900
PTK : EXN22_15135 EXN22_15885
PTAE : NCTC10697_02571(ybiC)
PIZ : LAB08_R21860 LAB08_R30880
PKJ : Q1W70_20890 Q1W70_21680 Q1W70_22710
PCUC : PSH97_10575 PSH97_13415
PBAM : NUH87_04930 NUH87_26275
PBEZ : SBP02_04095 SBP02_19555
PBUB : V6B39_13555 V6B39_15035
PSML : V6P94_13390 V6P94_14395
PSMZ : V6L79_13190 V6L79_14580
GAI : IMCC3135_33065(lhpD)
HBH : E4T21_06075 E4T21_12310
COBE : CLAM6_13330(lhpD_1) CLAM6_21120(lhpD_2)
COBB : H2O77_06845 H2O77_07170
COBD : U0O11_06505 U0O11_06725 U0O11_10600
CHJ : NCTC10426_00338(allD)
PLG : NCTC10937_02096(ybiC)
BPAR : BN117_1157 BN117_2289
BBH : BN112_0200 BN112_4460
BBM : BN115_2739 BN115_3632
BBX : BBS798_2214 BBS798_3736
MJE : LVC68_06010 LVC68_12445
EAW : ACEP9W_25875 ACEP9W_28945
RJG : CCGE525_00875 CCGE525_22370
PEM : OF122_01685 OF122_08990
ACUT : MRB58_03870 MRB58_09210(uraD)
BVY : NCTC9239_01937(ybiC)
TSV : DSM104635_03484(ybiC)
PAMI : JCM7686_1699 JCM7686_pAMI5p173
PARU : CYR75_05665 CYR75_12425
PPAN : ESD82_08915 ESD82_09045 ESD82_09100
PSEB : EOK75_09090 EOK75_15760 EOK75_17390
SPAG : sphantq_02874(dpkA)
PARH : I5S86_15500 I5S86_28205
» show all
Taxonomy
Reference
Authors
Payton CW, Chang YF
Title
delta1-piperideine-2-carboxylate reductase of Pseudomonas putida.
Journal
Reference
Authors
Muramatsu H, Mihara H, Kakutani R, Yasuda M, Ueda M, Kurihara T, Esaki N
Title
The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent delta1-piperideine-2-carboxylate/delta1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline.
Journal
Sequence
Reference
Authors
Watanabe S, Tanimoto Y, Yamauchi S, Tozawa Y, Sawayama S, Watanabe Y
Title
Identification and characterization of trans-3-hydroxy-l-proline dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.5.1.21
ExPASy - ENZYME nomenclature database: 1.5.1.21
LinkDB
All DBs