KEGG   ENZYME: 4.4.1.43
Entry
EC 4.4.1.43                 Enzyme                                 
Name
canavanine-gamma-lyase;
CangL
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
Sysname
L-canavanine N-hydroxyguanidine-lyase (L-homoserine-forming)
Reaction(IUBMB)
L-canavanine + H2O = L-homoserine + N-hydroxyguanidine (overall reaction) [RN:R13115];
(1a) L-canavanine = vinylglycine + N-hydroxyguanidine [RN:R13112];
(1b) vinylglycine = (2E)-2-aminobut-2-enoate (spontaneous) [RN:R13113];
(1c) (2E)-2-aminobut-2-enoate + H2O = L-homoserine (spontaneous) [RN:R13114]
Reaction(KEGG)
Substrate
L-canavanine [CPD:C00308];
H2O [CPD:C00001];
vinylglycine [CPD:C22624];
(2E)-2-aminobut-2-enoate [CPD:C22625]
Product
L-homoserine [CPD:C00263];
N-hydroxyguanidine [CPD:C22626];
vinylglycine [CPD:C22624];
(2E)-2-aminobut-2-enoate [CPD:C22625]
Comment
A pyridoxal 5'-phosphate protein. The enzyme, characterized from the bacterium Pseudomonas canavaninivorans, cleaves a carbon-oxygen bond, releasing N-hydroxyguanidine and an unstable enamine product that tautomerizes to an imine form, which is attacked by a water molecule to form L-homoserine.
History
EC 4.4.1.43 created 2022
Orthology
K26365  canavanine-gamma-lyase
Genes
VNAPN96_03100
VEJVEJY3_11085
VFUvfu_B00618
VFLAL536_01610
VGABSQ33_15705
VSRVspart_01493(mccB_1)
VZIG5S32_19085
VOSKNV97_03150
VRURND59_14575
PFEPSF113_2762
PFBVO64_0211
PTVAA957_03515
PFFPFLUOLIPICF723550
PBAPSEBR_a3032
PSILPMA3_09645
PKEDLD99_06065
PASGKSS96_14595
PALVKSS97_16230
PZAHU749_014965
PCASLOY40_15610
PPAELDL65_25045
TAUTola_1635
BCEDDM42_6464(megL)
BMECWJ16_10180
PTERC2L65_45090
PBRYNDK50_07405
HYLLPB072_00070
RGERGE_14420(metB)
SNNEWH46_17835
MAMOA6B35_32590
MHUAMCHK_11665 MCHK_7242
RHINGR_b03470(metB)
SFHSFHH103_06399(metB)
SFDUSDA257_c26390(mdeA2)
SAMESAMCFNEI73_pC1887(mdeA)
SINOSS05631_b52320
ESJSJ05684_b47920
EAKEKH55_4889 EKH55_5636 EKH55_5829
ENUPYH37_000757
AGCBSY240_1706(megL)
ALFCFBP5473_23990
RIRBN877_p0249(metB)
REPIE4803_CH03897
REIIE4771_CH03835
RLTRleg2_5066
RPHAAMC79_PD00749
RHKKim5_CH03866
RADCO657_28695
RROSD4A92_12050
RPATX73_013590
RPTRpal_2896
MOCBB934_32625
RVARvan_3389
RLACQMO75_13665
NOHG5V57_22075
SILSPO0413
RUTFIU92_00790(mdeA1)
SULIC1J05_17700
RHPLPB142_12680
GEHHYN69_15390
GFUKM031_11000
NSMJO391_10470
RMTIAI58_05215
RCVPFY06_20375
RAPRHOA_0180
RRURru_A0098
RRFF11_00495
AFWAnae109_4085
SURSTAUR_0514
AVMJQX13_40695
CFUSCYFUS_004892
CKLCKL_1632(metB2)
CKRCKR_1517
CPASClopa_2222
CPATCLPA_c22830(metB)
CPAECPAST_c22830(metB)
CLTCM240_0811
CTYKCTK_C14100(metB)
CDYF3K33_11340
RALRumal_2975
RUJE5Z56_00160
CAPREQM14_11875
SGYSgly_0928
ANVRBQ60_09360
CLEClole_4164
CEWEKH84_02320
ABUTAmi103574_05840
TTOThethe_01586
MEDMELS_1685
MANAMAMMFC1_00245(metB)
STEDSPTER_05340(megL)
CPRECsp1_01420(mgl_1)
GBRGbro_1986
GPOGPOL_c18850
GORKTR9_1917
GOQACH46_07535
GTABCM27_10300
GOCCXX93_15170
GITC6V83_08050
GRUGCWB2_09650(mdeA2)
GOMD7316_00499(mgl_1)
GAVC5O27_18105
GODGKZ92_09255
GAMGII34_08940
GPDGII33_08345
GJIH1R19_09540
GOILK459_00775
GHNMVF96_09690
GAMIIHQ52_12540
GSIP5P27_06125
DTMBJL86_1088
TOYFO059_15905
MIMAKG07_14025
MIHBJP65_12155
MHOSCXR34_13240
MFOLDXT68_01430
MCHNHCR76_17005
MAZANFX31_02490
MRGSM116_15510
AGMDCE93_05400
CARTPA27867_1930
SALCC2138_08010
SALDFVA74_07670
LYDD7I47_01150
MANTBHD05_08840
AOGLH407_12955
ARNCGK93_10275
ORNDV701_15935
BRIFDF13_07530
AJIC0Z10_12380
BROObrsh051_18780
NBTKLP28_12945
SACGFDZ84_25750 FDZ84_35495
SVISvir_19090
PDXPsed_3633
PSEEFRP1_14915
PSEHXF36_15135
PSEQAD006_22575
PECQAD017_02160
PHHAFB00_00095
PAUTPdca_41470
PBROHOP40_23260
PPELH6H00_21940
KBUQ4V64_03865
ACTYOG774_00550
BLOBL1559
BLBBBMN68_1590
BLZBLGT_09155
BDEBDP_0406(metB)
BDNBBDE_0388
BLEMBL8807_06145
BEUBE0216_05485
BSUEBS3272_00885
AGVOJF2_75610(mdeA_2)
TPITREPR_1228
TAZTREAZ_1603
PPIOCE91St28_02400
PYYRAH42_12685
EVIEchvi_4510
MAROMarbSA_07340
MBNMboo_1995
MPLMpal_0648
MAXMMALV_09500
MEUZKRP56_05405
 » show all
Reference
1  [PMID:36320885]
  Authors
Hauth F, Buck H, Stanoppi M, Hartig JS.
  Title
Canavanine utilization via homoserine and hydroxyguanidine by a PLP-dependent gamma-lyase in Pseudomonadaceae and Rhizobiales.
  Journal
RSC Chem Biol 3:1240-1250 (2022)
DOI:10.1039/d2cb00128d
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.4.1.43
IUBMB Enzyme Nomenclature: 4.4.1.43
ExPASy - ENZYME nomenclature database: 4.4.1.43
BRENDA, the Enzyme Database: 4.4.1.43
LinkDB

DBGET integrated database retrieval system