Contact and support
Need help, have a question, or want to contact the ResearchHub team?
© 2026 ResearchHub. Built for responsible scholarly connection.
Privacy-aware community infrastructureResearch graph
References from Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement. Local targets link to admitted publications; unresolved targets remain external evidence.
An appreciation of professor Alexander E. Braunstein. The discovery and scope of enzymatic transamination
10.1016/0300-9084(89)90169-7 · 1989 · External reference
Pyridoxal enzymes: mechanistic diversity and uniformity
10.1093/oxfordjournals.jbchem.a124931 · 1995 · External reference
10.1021/acscatal.7b02686
10.1021/acscatal.7b02686 · External reference
Controlling reaction specificity in pyridoxal phosphate enzymes
10.1016/j.bbapap.2011.05.019 · 2017 · External reference
10.1007/s00253-012-4103-3
10.1007/s00253-012-4103-3 · External reference
10.1134/s0006297917130028
10.1134/s0006297917130028 · External reference
10.1002/tcr.1021
10.1002/tcr.1021 · External reference
Microbial synthesis of (R)- and (S)-3,4-dimethoxyamphetamines through stereoselective transamination
10.1023/a:1026229610628 · 2003 · External reference
Microbial synthesis of chiral amines by (R)-specific transamination with Arthrobacter sp KNK168
10.1007/s00253-005-0002-1 · 2006 · External reference
ω-Transaminases for the synthesis of non-racemic α-chiral primary amines
10.1016/j.tibtech.2010.03.003 · 2010 · External reference
The industrial age of biocatalytic transamination
10.1002/ejoc.201500852 · 2015 · External reference
10.1039/c6gc02328b
10.1039/c6gc02328b · External reference
10.1007/s00253-011-3584-9
10.1007/s00253-011-3584-9 · External reference
A subfamily of PLP-dependent enzymes specialized in handling terminal amines
10.1016/j.bbapap.2015.02.023 · 2015 · External reference
Structural basis of the substrate range and enantioselectivity of two (S)-selective ω-transaminases
10.1021/acs.biochem.6b00370 · 2016 · External reference
Dual substrate recognition of aminotransferases
10.1002/tcr.20042 · 2005 · External reference
10.1006/jmbi.1998.1869
10.1006/jmbi.1998.1869 · External reference
The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity
10.1021/bi981921d · 1999 · External reference
Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5′-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme
10.1021/bi002769u · 2001 · External reference
Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition
10.1074/jbc.m311575200 · 2004 · External reference
Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme
10.1021/bi010384l · 2001 · External reference
Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme
10.1021/bi026722f · 2003 · External reference
10.1111/j.1742-4658.2012.08468.x
10.1111/j.1742-4658.2012.08468.x · External reference
10.1093/protein/gzs065
10.1093/protein/gzs065 · External reference
Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
10.1038/s41598-018-29846-0 · 2018 · External reference
Crystal structure of the apo form of a β-transaminase from Mesorhizobium sp. strain LUK
10.1002/pro.3594 · 2019 · External reference
Structural determinants of the β-selectivity of a bacterial aminotransferase
10.1074/jbc.m112.375238 · 2012 · External reference
10.1016/0022-2836(92)90691-c
10.1016/0022-2836(92)90691-c · External reference
In vitro characterization of the inhibitor resistance of glutamate-1-semialdehyde aminotransferase from the cyanobacterium Synechococcus PCC6301 GR6
10.1017/s0967026202003797 · 2002 · External reference
First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines
10.1007/s00792-016-0816-z · 2016 · External reference
Direct visualization of critical hydrogen atoms in a pyridoxal 5′-phosphate enzyme
10.1038/s41467-017-01060-y · 2017 · External reference
Hyperconjugation promotes catalysis in a pyridoxal 5′-phosphate-dependent enzyme
10.1021/acscatal.8b01911 · 2018 · External reference
Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine ε-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv
10.1016/j.jmb.2006.08.019 · 2006 · External reference
Structural and functional characterization of PseC, and aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori
10.1074/jbc.m512987200 · 2006 · External reference
A new target region for changing the substrate specificity of amine transaminases
10.1038/srep10753 · 2015 · External reference
Separation of L-leucine-pyruvate and L-leucine-α-ketoglutarate transaminases in Acetobacter suboxydans and identification of their reaction products
10.1080/00021369.1973.10860842 · 1973 · External reference
Purification and characterization of L-leucine-α-ketoglutarate transaminases from Acetobacter suboxydans
1976 · External reference
Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763
10.1128/aem.66.2.571-577.2000 · 2000 · External reference
Purification and partial characterization of the branched chain amino acid transaminase of Pseudomonas aeruginosa
10.1016/0005-2744(70)90109-9 · 1970 · External reference
A novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia
10.1016/j.enzmictec.2016.10.002 · 2017 · External reference
Properties of the bound coenzyme and subunit structure of omega-amino acid:pyruvate aminotransferase
10.1016/s0021-9258(18)32916-8 · 1983 · External reference
Crystal structure of pyridoxamine-pyruvate aminotransferase from Mesorhizobium loti MAFF303099
10.1074/jbc.m708061200 · 2008 · External reference
Characterization of amino acid aminotransferase of Methanococcus aeolicus
10.1128/jb.174.2.541-548.1992 · 1992 · External reference
10.1021/acscatal.6b02100
10.1021/acscatal.6b02100 · External reference
Folding and binding cascades: dynamic landscapes and population shifts
10.1110/ps.9.1.10 · 2000 · External reference
10.1016/j.sbi.2004.01.005
10.1016/j.sbi.2004.01.005 · External reference
10.1073/pnas.0507603102
10.1073/pnas.0507603102 · External reference
10.1126/science.1130258
10.1126/science.1130258 · External reference
10.1073/pnas.0802524105
10.1073/pnas.0802524105 · External reference
10.1073/pnas.0906966106
10.1073/pnas.0906966106 · External reference
Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray and NMR-resolved protein structures?
10.1002/prot.20491 · 2005 · External reference
10.2174/1874091x01004010083
10.2174/1874091x01004010083 · External reference
Oligomeric state and thermal stability of apo- and holo-human ornithine δ-aminotransferase
10.1007/s10930-017-9710-5 · 2017 · External reference
10.1073/pnas.44.2.98
10.1073/pnas.44.2.98 · External reference
10.1074/jbc.275.25.18939
10.1074/jbc.275.25.18939 · External reference
X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form
10.1093/oxfordjournals.jbchem.a124509 · 1994 · External reference
10.1073/pnas.181342398
10.1073/pnas.181342398 · External reference
Species dependence of enzyme-substrate encounter rates for triose phosphate isomerases
10.1002/(sici)1097-0134(19980601)31:4<406::aid-prot7>3.0.co;2-f · 1998 · External reference
Electrostatic steering and ionic tethering in enzyme-ligand binding: insights from simulations
10.1073/pnas.95.11.5942 · 1998 · External reference
10.1021/bi00053a003
10.1021/bi00053a003 · External reference
10.1126/science.3589666
10.1126/science.3589666 · External reference
10.1038/358347a0
10.1038/358347a0 · External reference
An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
10.1073/pnas.90.11.5128 · 1993 · External reference
